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Susumu Uchiyama - One of the best experts on this subject based on the ideXlab platform.
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Chromosome Protein framework from proteome analysis of isolated human metaphase Chromosomes
Chemical Record, 2007Co-Authors: Kiichi Fukui, Susumu UchiyamaAbstract:We have presented a structural model of the Chromosome based on its constituent Proteins. Development of a method of mass isolation for intact human metaphase Chromosomes and proteome analysis by mass spectrometry of the isolated chromosomal Proteins enabled us to develop a four-layer structural model of human metaphase Chromosomes. The model consists of four layers, each with different chromosomal Protein sets, i.e., Chromosome coating Proteins (CCPs), Chromosome peripheral Proteins (CPPs), Chromosome structural Proteins (CSPs), and Chromosome fibrous Proteins (CFPs). More than 200 identified Proteins have been classified and assigned to the four layers with each layer occupying a distinct region of the Chromosome. CCPs are localized at the most outer regions of the Chromosomes and they attach to the regions tentatively and occasionally. CCPs include mostly mitochondrial and cytoplasmic Proteins, e.g., 70 kDa heat shock Protein 9B and Hsp60. CPPs are also localized at the peripheral regions of the Chromosomes, but as the essential part of the Chromosomes. CPPs include nucleolin, lamin A/C, fibrillarin, etc. CSPs are the primary chromosomal structure Proteins, and include topoisomerase IIα, condensin subunits, histones, etc. CFPs have a fibrous nature, e.g., β-actin, vimentin, myosin II, tublin, etc. A data set of these Proteins, which we developed, contains essential Chromosome Proteins with classified information based on this four-layer model and presents useful leads for further studies on chromosomal structure and function. © 2007 The Japan Chemical Journal Forum and Wiley Periodicals, Inc. Chem Rec 7: 230–237; 2007: Published online in Wiley InterScience (www.interscience.wiley.com) DOI 10.1002/tcr.20120
Kiichi Fukui - One of the best experts on this subject based on the ideXlab platform.
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Chromosome Protein framework from proteome analysis of isolated human metaphase Chromosomes
Chemical Record, 2007Co-Authors: Kiichi Fukui, Susumu UchiyamaAbstract:We have presented a structural model of the Chromosome based on its constituent Proteins. Development of a method of mass isolation for intact human metaphase Chromosomes and proteome analysis by mass spectrometry of the isolated chromosomal Proteins enabled us to develop a four-layer structural model of human metaphase Chromosomes. The model consists of four layers, each with different chromosomal Protein sets, i.e., Chromosome coating Proteins (CCPs), Chromosome peripheral Proteins (CPPs), Chromosome structural Proteins (CSPs), and Chromosome fibrous Proteins (CFPs). More than 200 identified Proteins have been classified and assigned to the four layers with each layer occupying a distinct region of the Chromosome. CCPs are localized at the most outer regions of the Chromosomes and they attach to the regions tentatively and occasionally. CCPs include mostly mitochondrial and cytoplasmic Proteins, e.g., 70 kDa heat shock Protein 9B and Hsp60. CPPs are also localized at the peripheral regions of the Chromosomes, but as the essential part of the Chromosomes. CPPs include nucleolin, lamin A/C, fibrillarin, etc. CSPs are the primary chromosomal structure Proteins, and include topoisomerase IIα, condensin subunits, histones, etc. CFPs have a fibrous nature, e.g., β-actin, vimentin, myosin II, tublin, etc. A data set of these Proteins, which we developed, contains essential Chromosome Proteins with classified information based on this four-layer model and presents useful leads for further studies on chromosomal structure and function. © 2007 The Japan Chemical Journal Forum and Wiley Periodicals, Inc. Chem Rec 7: 230–237; 2007: Published online in Wiley InterScience (www.interscience.wiley.com) DOI 10.1002/tcr.20120
Michael J Welsh - One of the best experts on this subject based on the ideXlab platform.
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atp and amp mutually influence their interaction with the atp binding cassette abc adenylate kinase cystic fibrosis transmembrane conductance regulator cftr at separate binding sites
Journal of Biological Chemistry, 2013Co-Authors: Christoph O Randak, Qian Dong, Amanda Ver R Heul, Adrian H Elcock, Michael J WelshAbstract:Cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel in the ATP-binding cassette (ABC) transporter Protein family. In the presence of ATP and physiologically relevant concentrations of AMP, CFTR exhibits adenylate kinase activity (ATP + AMP ⇆ 2 ADP). Previous studies suggested that the interaction of nucleotide triphosphate with CFTR at ATP-binding site 2 is required for this activity. Two other ABC Proteins, Rad50 and a structural maintenance of Chromosome Protein, also have adenylate kinase activity. All three ABC adenylate kinases bind and hydrolyze ATP in the absence of other nucleotides. However, little is known about how an ABC adenylate kinase interacts with ATP and AMP when both are present. Based on data from non-ABC adenylate kinases, we hypothesized that ATP and AMP mutually influence their interaction with CFTR at separate binding sites. We further hypothesized that only one of the two CFTR ATP-binding sites is involved in the adenylate kinase reaction. We found that 8-azidoadenosine 5′-triphosphate (8-N3-ATP) and 8-azidoadenosine 5′-monophosphate (8-N3-AMP) photolabeled separate sites in CFTR. Labeling of the AMP-binding site with 8-N3-AMP required the presence of ATP. Conversely, AMP enhanced photolabeling with 8-N3-ATP at ATP-binding site 2. The adenylate kinase active center probe P1,P5-di(adenosine-5′) pentaphosphate interacted simultaneously with an AMP-binding site and ATP-binding site 2. These results show that ATP and AMP interact with separate binding sites but mutually influence their interaction with the ABC adenylate kinase CFTR. They further indicate that the active center of the adenylate kinase comprises ATP-binding site 2. Background: Cystic fibrosis transmembrane conductance regulator (CFTR) has adenylate kinase activity (ATP + AMP ⇆ 2 ADP). Results: ATP enables CFTR photolabeling by 8-N3-AMP, and AMP increases 8-N3-ATP photolabeling at ATP-binding site 2. Conclusion: AMP interacts with CFTR in an ATP-dependent manner and alters ATP interaction with the adenylate kinase active center ATP-binding site. Significance: These findings exemplify nucleotide interactions with an ABC adenylate kinase.
Fred H. Drake - One of the best experts on this subject based on the ideXlab platform.
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DNA topoisomerase II alpha is the major Chromosome Protein recognized by the mitotic phosphoProtein antibody MPM-2.
Proceedings of the National Academy of Sciences of the United States of America, 1993Co-Authors: Salme Taagepera, Fred H. DrakeAbstract:Abstract We have determined that the major mitotic phosphoProtein in Chromosomes recognized by the antiphosphoProtein antibody MPM-2 is the 170-kDa isoform of topoisomerase II (topo II), the isoform predominant in proliferating cells. As a prerequisite to making this discovery, it was necessary to develop protocols to protect chromosomal Proteins from dephosphorylation during cell extraction and Chromosome isolation procedures. Immunofluorescence analysis of the large Chromosomes prepared from Indian Muntjac cells revealed colocalization of MPM-2 and anti-topo II antibodies to the chromosomal centromeres and to the axial regions of the chromosomal arms. For biochemical fractionation studies, large quantities of Chromosomes from the P388D1 mouse lymphocyte cell line were isolated and treated to remove DNA and histone Proteins. Immunoblot and immunoprecipitation experiments with this Chromosome scaffold fraction identified the major MPM-2-reactive phosphoProtein to be DNA topo II. Using a panel of anti-peptide antibodies specific to the isoforms of topo II, we determined that the major phosphoProtein recognized by MPM-2 is the 170-kDa isoform of topo II, topo II alpha. The 180-kDa isoform, topo II beta, present in the isolated Chromosomes in much smaller quantities, is also recognized by MPM-2. The mitotic phosphorylation of the topo II Proteins may be critical for proper Chromosome condensation and segregation.
Salme Taagepera - One of the best experts on this subject based on the ideXlab platform.
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DNA topoisomerase II alpha is the major Chromosome Protein recognized by the mitotic phosphoProtein antibody MPM-2.
Proceedings of the National Academy of Sciences of the United States of America, 1993Co-Authors: Salme Taagepera, Fred H. DrakeAbstract:Abstract We have determined that the major mitotic phosphoProtein in Chromosomes recognized by the antiphosphoProtein antibody MPM-2 is the 170-kDa isoform of topoisomerase II (topo II), the isoform predominant in proliferating cells. As a prerequisite to making this discovery, it was necessary to develop protocols to protect chromosomal Proteins from dephosphorylation during cell extraction and Chromosome isolation procedures. Immunofluorescence analysis of the large Chromosomes prepared from Indian Muntjac cells revealed colocalization of MPM-2 and anti-topo II antibodies to the chromosomal centromeres and to the axial regions of the chromosomal arms. For biochemical fractionation studies, large quantities of Chromosomes from the P388D1 mouse lymphocyte cell line were isolated and treated to remove DNA and histone Proteins. Immunoblot and immunoprecipitation experiments with this Chromosome scaffold fraction identified the major MPM-2-reactive phosphoProtein to be DNA topo II. Using a panel of anti-peptide antibodies specific to the isoforms of topo II, we determined that the major phosphoProtein recognized by MPM-2 is the 170-kDa isoform of topo II, topo II alpha. The 180-kDa isoform, topo II beta, present in the isolated Chromosomes in much smaller quantities, is also recognized by MPM-2. The mitotic phosphorylation of the topo II Proteins may be critical for proper Chromosome condensation and segregation.