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Reinhard Luhrmann - One of the best experts on this subject based on the ideXlab platform.
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snrnp sm Proteins share two evolutionarily conserved sequence motifs which are involved in sm Protein Protein interactions
The EMBO Journal, 1995Co-Authors: H Hermann, Veronica A Raker, K Foulaki, H Hornig, H Brahms, Patrizia Fabrizio, Reinhard LuhrmannAbstract:Abstract The spliceosomal small nuclear ribonucleoProteins (snRNPs) U1, U2, U4/U6 and U5 share eight Proteins B', B, D1, D2, D3, E, F and G which form the structural core of the snRNPs. This class of common Proteins plays an essential role in the biogenesis of the snRNPs. In addition, these Proteins represent the major targets for the so-called anti-Sm auto-antibodies which are diagnostic for systemic lupus erythematosus (SLE). We have characterized the Proteins F and G from HeLa cells by cDNA cloning, and, thus, all human Sm Protein sequences are now available for comparison. Similar to the D, B/B' and E Proteins, the F and G Proteins do not possess any of the known RNA binding motifs, suggesting that other types of RNA-Protein interactions occur in the snRNP core. Strikingly, the eight human Sm Proteins possess mutual homology in two regions, 32 and 14 amino acids long, that we term Sm motifs 1 and 2. The Sm motifs are evolutionarily highly conserved in all of the putative homologues of the human Sm Proteins identified in the data base. These results suggest that the Sm Proteins may have arisen from a single common ancestor. Several hypothetical Proteins, mainly of plant origin, that clearly contain the conserved Sm motifs but exhibit only comparatively low overall homology to one of the human Sm Proteins, were identified in the data base. This suggests that the Sm motifs may also be shared by non-spliceosomal Proteins. Further, we provide experimental evidence that the Sm motifs are involved, at least in part, in Sm Protein-Protein interactions. Specifically, we show by co-immunoprecipitation analyses of in vitro translated B' and D3 that the Sm motifs are essential for complex formation between B' and D3. Our finding that the Sm Proteins share conserved sequence motifs may help to explain the frequent occurrence in patient sera of anti-Sm antibodies that cross-react with multiple Sm Proteins and may ultimately further our understanding of how the snRNPs act as auto-antigens and immunogens in SLE.
Michael Feig - One of the best experts on this subject based on the ideXlab platform.
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effect of Protein Protein interactions and solvent viscosity on the rotational diffusion of Proteins in crowded environments
Physical Chemistry Chemical Physics, 2019Co-Authors: Grzegorz Nawrocki, Alp Karaboga, Yuji Sugita, Michael FeigAbstract:The rotational diffusion of a Protein in the presence of Protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct Protein–Protein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key Protein–Protein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given Protein and the resulting propensity for forming interactions with surrounding Proteins in a crowded cellular environment may be the major determinant of its diffusive properties.
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Effect of Protein–Protein interactions and solvent viscosity on the rotational diffusion of Proteins in crowded environments
Physical Chemistry Chemical Physics, 2019Co-Authors: Grzegorz Nawrocki, Alp Karaboga, Yuji Sugita, Michael FeigAbstract:The rotational diffusion of a Protein in the presence of Protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct Protein–Protein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key Protein–Protein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given Protein and the resulting propensity for forming interactions with surrounding Proteins in a crowded cellular environment may be the major determinant of its diffusive properties.
H Hermann - One of the best experts on this subject based on the ideXlab platform.
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snrnp sm Proteins share two evolutionarily conserved sequence motifs which are involved in sm Protein Protein interactions
The EMBO Journal, 1995Co-Authors: H Hermann, Veronica A Raker, K Foulaki, H Hornig, H Brahms, Patrizia Fabrizio, Reinhard LuhrmannAbstract:Abstract The spliceosomal small nuclear ribonucleoProteins (snRNPs) U1, U2, U4/U6 and U5 share eight Proteins B', B, D1, D2, D3, E, F and G which form the structural core of the snRNPs. This class of common Proteins plays an essential role in the biogenesis of the snRNPs. In addition, these Proteins represent the major targets for the so-called anti-Sm auto-antibodies which are diagnostic for systemic lupus erythematosus (SLE). We have characterized the Proteins F and G from HeLa cells by cDNA cloning, and, thus, all human Sm Protein sequences are now available for comparison. Similar to the D, B/B' and E Proteins, the F and G Proteins do not possess any of the known RNA binding motifs, suggesting that other types of RNA-Protein interactions occur in the snRNP core. Strikingly, the eight human Sm Proteins possess mutual homology in two regions, 32 and 14 amino acids long, that we term Sm motifs 1 and 2. The Sm motifs are evolutionarily highly conserved in all of the putative homologues of the human Sm Proteins identified in the data base. These results suggest that the Sm Proteins may have arisen from a single common ancestor. Several hypothetical Proteins, mainly of plant origin, that clearly contain the conserved Sm motifs but exhibit only comparatively low overall homology to one of the human Sm Proteins, were identified in the data base. This suggests that the Sm motifs may also be shared by non-spliceosomal Proteins. Further, we provide experimental evidence that the Sm motifs are involved, at least in part, in Sm Protein-Protein interactions. Specifically, we show by co-immunoprecipitation analyses of in vitro translated B' and D3 that the Sm motifs are essential for complex formation between B' and D3. Our finding that the Sm Proteins share conserved sequence motifs may help to explain the frequent occurrence in patient sera of anti-Sm antibodies that cross-react with multiple Sm Proteins and may ultimately further our understanding of how the snRNPs act as auto-antigens and immunogens in SLE.
Grzegorz Nawrocki - One of the best experts on this subject based on the ideXlab platform.
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effect of Protein Protein interactions and solvent viscosity on the rotational diffusion of Proteins in crowded environments
Physical Chemistry Chemical Physics, 2019Co-Authors: Grzegorz Nawrocki, Alp Karaboga, Yuji Sugita, Michael FeigAbstract:The rotational diffusion of a Protein in the presence of Protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct Protein–Protein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key Protein–Protein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given Protein and the resulting propensity for forming interactions with surrounding Proteins in a crowded cellular environment may be the major determinant of its diffusive properties.
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Effect of Protein–Protein interactions and solvent viscosity on the rotational diffusion of Proteins in crowded environments
Physical Chemistry Chemical Physics, 2019Co-Authors: Grzegorz Nawrocki, Alp Karaboga, Yuji Sugita, Michael FeigAbstract:The rotational diffusion of a Protein in the presence of Protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct Protein–Protein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key Protein–Protein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given Protein and the resulting propensity for forming interactions with surrounding Proteins in a crowded cellular environment may be the major determinant of its diffusive properties.
Angus S Murphy - One of the best experts on this subject based on the ideXlab platform.
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post transcriptional regulation of auxin transport Proteins cellular trafficking Protein phosphorylation Protein maturation ubiquitination and membrane composition
Journal of Experimental Botany, 2009Co-Authors: Boosaree Titapiwatanakun, Angus S MurphyAbstract:Auxin concentration gradients, established by polar transport of auxin, are essential for the establishment and maintenance of polar growth and morphological patterning. Three families of cellular transport Proteins, PIN-formed (PIN), P-glycoProtein (ABCB/PGP), and AUXIN RESISTANT 1/LIKE AUX1 (AUX1/LAX), can independently and coordinately transport auxin in plants. Regulation of these Proteins involves intricate and co-ordinated cellular processes, including Protein‐Protein interactions, vesicular trafficking, Protein phosphorylation, ubiquitination, and stabilization of the transporter complexes on the plasma membrane.
