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Su Hao Lo - One of the best experts on this subject based on the ideXlab platform.
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Tensin regulates pharyngeal pumping in Caenorhabditis elegans.
Biochemical and Biophysical Research Communications, 2019Co-Authors: Aaron N. Bruns, Su Hao LoAbstract:Abstract Tensin is a focal adhesion molecule that is known to regulate cell adhesion, migration, and proliferation. Although there are four Tensin homologs (TNS1, TNS2, TNS3, and CTEN/TNS4) in mammals, only one Tensin gene is found in Caenorhabditis elegans. Sequence analysis suggests that Caenorhabditis elegans Tensin is slightly closer aligned with human TNS1 than with other human Tensins. To establish the role of TNS1 in Caenorhabditis elegans, we have generated TNS1 knockout (KO) worms by CRISPR-Cas9 and homologous recombination directed repair approaches. Lack of TNS1 does not appear to affect the development or gross morphology of the worms. Nonetheless, defecation cycles are significantly longer in TNS1 KO worms. In addition, their pharyngeal pumping rate is markedly faster, which is likely due to a shorter pump duration in the KO worms. These findings indicate that TNS1 is not required for the development and survival of Caenorhabditis elegans but point to a critical role in modulating defecation and pharyngeal pumping rates.
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C-terminal Tensin-like (CTEN): a promising biomarker and target for cancer.
The International Journal of Biochemistry & Cell Biology, 2014Co-Authors: Su Hao LoAbstract:C-terminal Tensin-like (cten, also known as Tensin4, TNS4) is a member of the Tensin family. Cten protein, like the other three Tensin family members, localizes to focal adhesion sites but only shares sequence homology with other Tensins at its C-terminal region, which contains the SH2 and PTB domains. Cten is abundantly expressed in normal prostate and placenta and is down-regulated in prostate cancer. However, overexpression of cten frequently associates with tumors derived from breast, colon, lung, stomach, skin and pancreas. A variety of cancer-associated growth factors and cytokines induce cten expression. Up-regulated cten promotes cell motility, prolongs epidermal growth factor receptor signaling, and enhances tumorigenicity. Emerging findings suggest that cten is a promising biomarker and therapeutic target for various cancers.
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Association of the Tensin N-terminal Protein-tyrosine Phosphatase Domain with the α Isoform of Protein Phosphatase-1 in Focal Adhesions
Journal of Biological Chemistry, 2007Co-Authors: Jason A. Kirkbride, Su Hao Lo, Elizabeth Elliott, David L. BrautiganAbstract:Abstract Focal adhesions attach cultured cells to the extracellular matrix, and we found endogenous protein phosphatase-1α isoform (PP1α) localized in adhesions across the entire area of adherent fibroblasts. However, in fibroblasts migrating into a scrape wound or spreading after replating PP1α did not appear in adhesions near the leading edge but was recruited into other adhesions coincident in time and space with incorporation of Tensin. Endogenous Tensin and PP1α co-precipitated from cell lysates with isoform-specific PP1 antibodies. Chemical cross-linking of focal adhesion preparations with Lomant's reagent demonstrated molecular proximity of endogenous PP1α and Tensin, whereas neither focal adhesion kinase nor vinculin was cross-linked and co-precipitated with PP1α, suggesting distinct spatial subdomains within adhesions. Transient expression of truncated Tensin showed the N-terminal 360 residues, which comprise a protein-tyrosine phosphatase domain, alone were sufficient for isoform-selective co-precipitation of co-expressed PP1α. Human prostate cancer PC3 cells are deficient in Tensin relative to fibroblasts and have fewer, mostly peripheral adhesions. Transient expression of green fluorescent protein Tensin in these cancer cells induced formation of adhesions and recruited endogenous PP1α into those adhesions. Thus, the protein-tyrosine phosphatase domain of Tensin exhibits isoform-specific association with PP1α in a restricted spatial region of adhesions that are formed during cell migration.
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Epidermal growth factor modulates tyrosine phosphorylation of a novel Tensin family member, Tensin3.
Molecular Cancer Research, 2004Co-Authors: Yi Chun Liao, Su Hao LoAbstract:Here, we report the identification of a new Tensin family member, Tensin3, and its role in epidermal growth factor (EGF) signaling pathway. Human Tensin3 cDNA encodes a 1445 amino acid sequence that shares extensive homology with Tensin1, Tensin2, and COOH-terminal Tensin-like protein. Tensin3 is expressed in various tissues and in different cell types such as endothelia, epithelia, and fibroblasts. The potential role of Tensin3 in EGF-induced signaling pathway is explored. EGF induces tyrosine phosphorylation of Tensin3 in MDA-MB-468 cells in a time- and dose-dependent manner, but it is independent of an intact actin cytoskeleton or phosphatidylinositol 3-kinase. Activation of EGF receptor is necessary but not sufficient for tyrosine phosphorylation of Tensin3. It also requires Src family kinase activities. Furthermore, Tensin3 forms a complex with focal adhesion kinase and p130Cas in MDA-MB-468 cells. Addition of EGF to the cells induces dephosphorylation of these two molecules, leads to disassociation of the Tensin3-focal adhesion kinase-p130Cas complex, and enhances the interaction between Tensin3 and EGF receptor. Our results demonstrate that Tensin3 may function as a platform for the disassembly of EGF-related signaling complexes at focal adhesions.
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Regulation of Tensin-promoted cell migration by its focal adhesion binding and Src homology domain 2.
Biochemical Journal, 2003Co-Authors: Huaiyang Chen, Su Hao LoAbstract:Tensin1 is an actin- and phosphotyrosine-binding protein that localizes to focal adhesions. Recently, we have shown that both Tensin1 and a new family member, Tensin2, promote cell migration [Chen, Duncan, Bozorgchami and Lo (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 733-738]. Since localization of proteins to particular intracellular compartments often regulates their functions, and Src homology domain 2 may mediate signals related to cell migration, we hypothesize that Tensin-mediated cell migration is regulated by the focal adhesion localization and the Src homology domain 2 of Tensin. To test this hypothesis, we have analysed the effects of a series of Tensin1 mutants on cell migration. Our results have shown that (1) Tensin1 contains two focal adhesion-binding sites, (2) the wild-type Tensin1 significantly promotes cell migration, (3) mutants with one focal adhesion-binding site do not promote cell migration, (4) the non-focal adhesion localized mutant suppresses cell migration and (5) the mutant that is not able to bind to phosphotyrosine-containing proteins has no effect on cell migration. These results have indicated that focal adhesion localization of Tensin1 and the phosphotyrosine-binding activity are two critical factors in regulating Tensin-mediated cell migration.
Douglas R Lowy - One of the best experts on this subject based on the ideXlab platform.
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the Tensin 3 protein including its sh2 domain is phosphorylated by src and contributes to tumorigenesis and metastasis
Cancer Cell, 2009Co-Authors: Xiaolan Qian, Guorong Li, Laura Asnaghi, William C Vass, Alex G Papageorge, Renard C Walker, Peter J Steinbach, Giovanna Tosato, Kent Hunter, Douglas R LowyAbstract:Summary In cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous Tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the Tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of Tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, Tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous Tensin-3. Thus, Tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding.
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oncogenic inhibition by a deleted in liver cancer gene requires cooperation between Tensin binding and rho specific gtpase activating protein activities
Proceedings of the National Academy of Sciences of the United States of America, 2007Co-Authors: Xiaolan Qian, Kenneth M Yamada, Guorong Li, Holly K Asmussen, Laura Asnaghi, William C Vass, Richard Braverman, Nicholas C Popescu, Alex G Papageorge, Douglas R LowyAbstract:The three deleted in liver cancer genes (DLC1–3) encode Rho-GTPase-activating proteins (RhoGAPs) whose expression is frequently down-regulated or silenced in a variety of human malignancies. The RhoGAP activity is required for full DLC-dependent tumor suppressor activity. Here we report that DLC1 and DLC3 bind to human Tensin1 and its chicken homolog. The binding has been mapped to the Tensin Src homology 2 (SH2) and phosphotyrosine binding (PTB) domains at the C terminus of Tensin proteins. Distinct DLC1 sequences are required for SH2 and PTB binding. DCL binding to both domains is constitutive under basal conditions. The SH2 binding depends on a tyrosine in DCL1 (Y442) but is phosphotyrosine-independent, a highly unusual feature for SH2 binding. DLC1 competed with the binding of other proteins to the Tensin C terminus, including β3-integrin binding to the PTB domain. Point mutation of a critical tyrosine residue (Y442F) in DLC1 rendered the protein deficient for binding the Tensin SH2 domain and binding full-length Tensin. The Y442F protein was diffusely cytoplasmic, in contrast to the localization of wild-type DLC1 to focal adhesions, but it retained the ability to reduce the intracellular levels of Rho-GTP. The Y442F mutant displayed markedly reduced biological activity, as did a mutant that was RhoGAP-deficient. The results suggest that DLC1 is a multifunctional protein whose biological activity depends on cooperation between its Tensin binding and RhoGAP activities, although neither activity depends on the other.
Jan Sorensen - One of the best experts on this subject based on the ideXlab platform.
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structure production characteristics and fungal antagonism of Tensin a new antifungal cyclic lipopeptide from pseudomonas fluorescens strain 96 578
Journal of Applied Microbiology, 2000Co-Authors: Tommy Harder Nielsen, C Thrane, Carsten Christophersen, Uffe Anthoni, Jan SorensenAbstract:Aim: To study the antagonistic activity by Pseudomonas fluorescens strain 96.578 on the plant pathogenic fungus Rhizoctonia solani. Methods and Results: Strain 96.578 produced a new cyclic lipopeptide, Tensin. High Tensin production per cell was detected in liquid media with glucose, mannitol or glutamate as growth substrate while fructose, sucrose and asparagine supported low production. Tensin production was nearly constant in media with different initial C levels, while low initial N contents reduced production. When applied to sugar beet seeds, strain 96.578 produced Tensin during seed germination. When challenged with strain 96.578 or purified Tensin, Rhizoctonia solani reduced radial mycelium extension but increased branching and rosette formation. Conclusion: The antagonistic activity of strain 96.578 towards Rhizoctonia solani was caused by Tensin. Significance and Impact of the Study: When coated onto sugar beet seeds, Tensin production by strain 96.578 could be of significant importance for inhibition of mycelial growth and seed infection by Rhizoctonia solani.
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Structure, production characteristics and fungal antagonism of Tensin – a new antifungal cyclic lipopeptide from Pseudomonas fluorescens strain 96.578
Journal of Applied Microbiology, 2000Co-Authors: Tommy Harder Nielsen, C Thrane, Carsten Christophersen, Uffe Anthoni, Jan SorensenAbstract:Aim: To study the antagonistic activity by Pseudomonas fluorescens strain 96.578 on the plant pathogenic fungus Rhizoctonia solani. Methods and Results: Strain 96.578 produced a new cyclic lipopeptide, Tensin. High Tensin production per cell was detected in liquid media with glucose, mannitol or glutamate as growth substrate while fructose, sucrose and asparagine supported low production. Tensin production was nearly constant in media with different initial C levels, while low initial N contents reduced production. When applied to sugar beet seeds, strain 96.578 produced Tensin during seed germination. When challenged with strain 96.578 or purified Tensin, Rhizoctonia solani reduced radial mycelium extension but increased branching and rosette formation. Conclusion: The antagonistic activity of strain 96.578 towards Rhizoctonia solani was caused by Tensin. Significance and Impact of the Study: When coated onto sugar beet seeds, Tensin production by strain 96.578 could be of significant importance for inhibition of mycelial growth and seed infection by Rhizoctonia solani.
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Cyclic lipoundecapeptide Tensin from Pseudomonas fluorescens strain 96.578.
Acta Crystallographica Section C-crystal Structure Communications, 2000Co-Authors: Anette Henriksen, Tommy Harder Nielsen, Carsten Christophersen, Uffe Anthoni, Jan Sorensen, Michael GajhedeAbstract:The crystal structure of the non-ribosomal lipoundecapeptide Tensin from Pseudomonas fluorescens has been solved as an ethyl acetate/bis-water solvate (Tensin ethyl acetate dihydrate, C67H115N12O20·C4H8O2·2H2O) to a resolution of 0.8 A. The primary structure of Tensin is β-hydroxydecanoyl-d-Leu-d-Asp-d-allo-Thr-d-Leu-d-Leu-d-Ser-l-Leu-d-Gln-l-Leu-l-Ile-l-Glu. The peptide is a lactone linking the Thr3 Oγ atom to the C-terminal C atom. The stereochemistry of the β-hydroxy acid has been shown to be S. The peptide shows structural resemblance to the non-ribosomal cyclic lipopeptide fengycin from Bacillus subtilis. The structure of Tensin is essentially helical (310-helix), with the cyclic peptide wrapping around a hydrogen-bonded water molecule. The lipopeptide is amphipathic in good agreement with its function as a biosurfactant.
Lan Bo Chen - One of the best experts on this subject based on the ideXlab platform.
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Molecular characterization of human Tensin.
Biochemical Journal, 2000Co-Authors: Huaiyang Chen, Akiko Ishii, Wai-keung Wong, Lan Bo Chen, Su Hao LoAbstract:Tensin is a focal-adhesion molecule that binds to actin filaments and interacts with phosphotyrosine-containing proteins. To analyse Tensin9s function in mammals, we have cloned Tensin cDNAs from human and cow. The isolated approx. 7.7-kb human cDNA contains an open reading frame encoding 1735 amino acid residues. The amino acid sequence of human Tensin shares 60% identity with chicken Tensin, and contains all the structural features described previously in chicken Tensin. This includes the actin-binding domains, the Src homology domain 2, and the region similar to a tumour suppressor, PTEN. Two major differences between human and chicken Tensin are (i) the lack of the first 54 residues present in chicken Tensin, and (ii) the addition of 34- and 38-residue inserts in human and bovine Tensin. In addition, our interspecies sequencing data have uncovered the presence of a glutamine/CAG repeat that appears to have expanded in the course of evolution. Northern-blot analysis reveals a 10-kb message in most of the human tissues examined. An additional 9-kb message is detected in heart and skeletal muscles. The molecular mass predicted from the human cDNA is 185kDa, although both endogenous and recombinant human Tensin migrate as 220-kDa proteins on SDS/PAGE. The discrepancy is due to the unusually low electrophoretic mobility of the central region of the Tensin polypeptide (residues 306–981). A survey of human prostate and breast cancer cell lines by Western-blot analysis shows a lack of Tensin expression in most cancer cell lines, whereas these lines express considerable amounts of focal-adhesion molecules such as talin and focal-adhesion kinase. Finally, Tensin is rapidly cleaved by a focal-adhesion protease, calpain II. Incubation of cells with a calpain inhibitor, MDL, prevented Tensin cleavage and induced morphological change in these cells, suggesting that cleavage of Tensin and other focal-adhesion constituents by calpain disrupts maintenance of normal cell shape.
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progressive kidney degeneration in mice lacking Tensin
Journal of Cell Biology, 1997Co-Authors: Su Hao Lo, Lan Bo Chen, Qianchun Yu, Linda Degenstein, Elaine FuchsAbstract:Tensin is a focal adhesion phosphoprotein that binds to F-actin and contains a functional Src homology 2 domain. To explore the biological functions of Tensin, we cloned the mouse Tensin gene, determined its program of expression, and used gene targeting to generate mice lacking Tensin. Even though Tensin is expressed in many different tissues during embryogenesis, Tensin null mice developed normally and appeared healthy postnatally for at least several months. Over time, −/− mice became frail because of abnormalities in their kidneys, an organ that expresses high levels of Tensin. Mice with overt signs of weakness exhibited signs of renal failure and possessed multiple large cysts in the proximal kidney tubules, but even in Tensin null mice with normal blood analysis, cysts were prevalent. Ultrastructurally, noncystic areas showed typical cell– matrix junctions that readily labeled with antibodies against other focal adhesion molecules. In abnormal regions, cell–matrix junctions were disrupted and tubule cells lacked polarity. Taken together, our data imply that, in the kidney, loss of Tensin leads to a weakening, rather than a severing, of focal adhesion. All other tissues appeared normal, suggesting that, in most cases, Tensin's diverse functions are redundant and may be compensated for by other focal adhesion proteins.
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Platelet-derived Growth Factor-induced Formation of Tensin and Phosphoinositide 3-Kinase Complexes
Journal of Biological Chemistry, 1996Co-Authors: Kurt R. Auger, Su Hao Lo, Zhou Songyang, Thomas M. Roberts, Lan Bo ChenAbstract:Tensin is an SH2 domain-containing cytoskeletal protein that binds to and caps actin filaments. Investigation of signal transduction mechanisms associated with Tensin revealed the presence of phosphoinositide 3-kinase (PI 3-kinase) activity in Tensin immunoprecipitates from platelet-derived growth factor-treated cells. Association of PI 3-kinase activity with Tensin was transitory, and the amount of activity was approximately 1% of the total PI 3-kinase activity found in anti-phosphotyrosine (anti-pY) immunoprecipitates. In vitro, PI 3-kinase activity associated with the SH2 domain of Tensin in a platelet-derived growth factor-dependent manner. The optimal phosphopeptide binding specificity of the SH2 domain of Tensin was determined to be phospho-Y (E or D), N, (I, V, or F). Synthetic phosphopeptides containing the sequence YENI could specifically block the association of PI 3-kinase activity with Tensin in a dose-dependent manner. These results suggest that PI 3-kinase interacts with the cytoskeleton via the SH2 domain of Tensin and may play an important role in platelet-derived growth factor-induced cytoskeletal reorganization that is concomitant with cell migration and proliferation.
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Tensin a potential link between the cytoskeleton and signal transduction
BioEssays, 1994Co-Authors: Su Hao Lo, Ellen Weisberg, Lan Bo ChenAbstract:Cytoskeletal proteins provide the structural foundation that allows cells to exist in a highly organized manner. Recent evidence suggests that certain cytoskeletal proteins not only maintain structural integrity, but might also be associated with signal transduction and suppression of tumorigenesis. Since the time of the discovery of Tensin, a fair amount of data has been gathered which supports the notion that Tensin is one such protein possessing these characteristics. In this review, we discuss recent studies that: (1) elucidate a role for Tensin in maintenance of cellular structure and signal transduction; (2) implicate Tensin as the anchor for actin filaments at the focal adhesion; (3) describe the phosphorylation of Tensin; (4) describe potential targets for its Src homology region 2 domain; (5) describe the association between Tensin and the nuclear protein p130; and (6) demonstrate that increased Tensin expression in a cell line appears to reduce its transformation potential.
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Molecular cloning of chick cardiac muscle Tensin. Full-length cDNA sequence, expression, and characterization.
Journal of Biological Chemistry, 1994Co-Authors: Su Hao Lo, Wai-keung Wong, Paul A Janmey, John H Hartwig, Qi An, Lan Bo ChenAbstract:Abstract Here we describe the molecular cloning of 7.1-kilobase cDNA encoding chick cardiac muscle Tensin. It contains an open reading frame of 1,744 amino acid (aa) residues. Sequence analysis reveals that, in addition to the previously noted SH2 domain (Davis, S., Lu, M. L., Lo, S. H., Lin, S., Butler, J. A., Druker, B. J., Roberts, T. M., An, Q., and Chen, L. B. (1991) Science 252, 712-715), Tensin contains virtually all of the known sequence (362 aa) of insertin, an actin-capping protein that allows actin monomer to be "inserted" (Schroer, E., and Wegner, A. (1985) Eur. J. Biochem. 153, 515-520). Moreover, Tensin shares partial homology with actin (46.7% identity in 30 aa), beta-spectrin's actin-binding consensus (40% identity in 26 aa), BCR (40% identity in 25 aa), catenin alpha (35% identity in 45 aa), synapsin Ia (25.6% identity in 156 aa), IL-3 receptor (20.2% identity in 384 aa), and IL-2/EPO receptors (14% identity in 20 aa). Recombinant full-length Tensin, tagged with an influenza-derived epitope, was over-expressed by a baculovirus system and purified to apparent homogeneity. It migrates as a 200-kDa protein in SDS-polyacrylamide gel electrophoresis, similar to the native Tensin. The structure of the Tensin molecule has been characterized by light scattering, electron microscopy, and gel filtration. Nine monoclonal antibodies recognizing different regions of Tensin have been prepared and characterized. The epitope-tagged recombinant Tensin gene was subcloned into a pRcCMV vector and transfected into NIH 3T3 cells. Immunofluorescence stainings with monoclonal antibodies specific for chick Tensin (not cross-reactive with mouse Tensin) showed that the expressed protein is indeed localized at focal contacts, as that of native Tensin.
Tommy Harder Nielsen - One of the best experts on this subject based on the ideXlab platform.
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structure production characteristics and fungal antagonism of Tensin a new antifungal cyclic lipopeptide from pseudomonas fluorescens strain 96 578
Journal of Applied Microbiology, 2000Co-Authors: Tommy Harder Nielsen, C Thrane, Carsten Christophersen, Uffe Anthoni, Jan SorensenAbstract:Aim: To study the antagonistic activity by Pseudomonas fluorescens strain 96.578 on the plant pathogenic fungus Rhizoctonia solani. Methods and Results: Strain 96.578 produced a new cyclic lipopeptide, Tensin. High Tensin production per cell was detected in liquid media with glucose, mannitol or glutamate as growth substrate while fructose, sucrose and asparagine supported low production. Tensin production was nearly constant in media with different initial C levels, while low initial N contents reduced production. When applied to sugar beet seeds, strain 96.578 produced Tensin during seed germination. When challenged with strain 96.578 or purified Tensin, Rhizoctonia solani reduced radial mycelium extension but increased branching and rosette formation. Conclusion: The antagonistic activity of strain 96.578 towards Rhizoctonia solani was caused by Tensin. Significance and Impact of the Study: When coated onto sugar beet seeds, Tensin production by strain 96.578 could be of significant importance for inhibition of mycelial growth and seed infection by Rhizoctonia solani.
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Structure, production characteristics and fungal antagonism of Tensin – a new antifungal cyclic lipopeptide from Pseudomonas fluorescens strain 96.578
Journal of Applied Microbiology, 2000Co-Authors: Tommy Harder Nielsen, C Thrane, Carsten Christophersen, Uffe Anthoni, Jan SorensenAbstract:Aim: To study the antagonistic activity by Pseudomonas fluorescens strain 96.578 on the plant pathogenic fungus Rhizoctonia solani. Methods and Results: Strain 96.578 produced a new cyclic lipopeptide, Tensin. High Tensin production per cell was detected in liquid media with glucose, mannitol or glutamate as growth substrate while fructose, sucrose and asparagine supported low production. Tensin production was nearly constant in media with different initial C levels, while low initial N contents reduced production. When applied to sugar beet seeds, strain 96.578 produced Tensin during seed germination. When challenged with strain 96.578 or purified Tensin, Rhizoctonia solani reduced radial mycelium extension but increased branching and rosette formation. Conclusion: The antagonistic activity of strain 96.578 towards Rhizoctonia solani was caused by Tensin. Significance and Impact of the Study: When coated onto sugar beet seeds, Tensin production by strain 96.578 could be of significant importance for inhibition of mycelial growth and seed infection by Rhizoctonia solani.
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Cyclic lipoundecapeptide Tensin from Pseudomonas fluorescens strain 96.578.
Acta Crystallographica Section C-crystal Structure Communications, 2000Co-Authors: Anette Henriksen, Tommy Harder Nielsen, Carsten Christophersen, Uffe Anthoni, Jan Sorensen, Michael GajhedeAbstract:The crystal structure of the non-ribosomal lipoundecapeptide Tensin from Pseudomonas fluorescens has been solved as an ethyl acetate/bis-water solvate (Tensin ethyl acetate dihydrate, C67H115N12O20·C4H8O2·2H2O) to a resolution of 0.8 A. The primary structure of Tensin is β-hydroxydecanoyl-d-Leu-d-Asp-d-allo-Thr-d-Leu-d-Leu-d-Ser-l-Leu-d-Gln-l-Leu-l-Ile-l-Glu. The peptide is a lactone linking the Thr3 Oγ atom to the C-terminal C atom. The stereochemistry of the β-hydroxy acid has been shown to be S. The peptide shows structural resemblance to the non-ribosomal cyclic lipopeptide fengycin from Bacillus subtilis. The structure of Tensin is essentially helical (310-helix), with the cyclic peptide wrapping around a hydrogen-bonded water molecule. The lipopeptide is amphipathic in good agreement with its function as a biosurfactant.
