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rdf:type |
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lifeskim:mentions |
umls-concept:C0007709,
umls-concept:C0055060,
umls-concept:C0205147,
umls-concept:C0332256,
umls-concept:C0475264,
umls-concept:C1273518,
umls-concept:C1413340,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
7
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pubmed:dateCreated |
2004-2-9
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pubmed:abstractText |
Recently, human artificial chromosomes featuring functional centromeres have been generated efficiently from naked synthetic alphoid DNA containing CENP-B boxes as a de novo mechanism in a human cultured cell line, but not from the synthetic alphoid DNA only containing mutations within CENP-B boxes, indicating that CENP-B has some functions in assembling centromere/kinetochore components on alphoid DNA. To investigate whether any interactions exist between CENP-B and the other centromere proteins, we screened a cDNA library by yeast two-hybrid analysis. An interaction between CENP-B and CENP-C was detected, and the CENP-C domains required were determined to overlap with three Mif2 homologous regions, which were also revealed to be involved in the CENP-C assembly of centromeres by expression of truncated polypeptides in cultured cells. Overproduction of truncated CENP-B containing no CENP-C interaction domains caused abnormal duplication of CENP-C domains at G2 and cell cycle delay at metaphase. These results suggest that the interaction between CENP-B and CENP-C may be involved in the correct assembly of CENP-C on alphoid DNA. In other words, a possible molecular linkage may exist between one of the kinetochore components and human centromere DNA through CENP-B/CENP-B box interaction.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/CENPB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Centromere Protein B,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Demecolcine,
http://linkedlifedata.com/resource/pubmed/chemical/MIF2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/centromere protein C
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5934-46
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14612452-Autoantigens,
pubmed-meshheading:14612452-Cell Line,
pubmed-meshheading:14612452-Cell Nucleus,
pubmed-meshheading:14612452-Centromere,
pubmed-meshheading:14612452-Centromere Protein B,
pubmed-meshheading:14612452-Chromatin,
pubmed-meshheading:14612452-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:14612452-Cloning, Molecular,
pubmed-meshheading:14612452-DNA,
pubmed-meshheading:14612452-DNA, Complementary,
pubmed-meshheading:14612452-DNA-Binding Proteins,
pubmed-meshheading:14612452-Demecolcine,
pubmed-meshheading:14612452-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:14612452-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:14612452-G2 Phase,
pubmed-meshheading:14612452-Gene Library,
pubmed-meshheading:14612452-HeLa Cells,
pubmed-meshheading:14612452-Humans,
pubmed-meshheading:14612452-Kinetochores,
pubmed-meshheading:14612452-Metaphase,
pubmed-meshheading:14612452-Microscopy, Phase-Contrast,
pubmed-meshheading:14612452-Mutation,
pubmed-meshheading:14612452-Peptides,
pubmed-meshheading:14612452-Plasmids,
pubmed-meshheading:14612452-Precipitin Tests,
pubmed-meshheading:14612452-Protein Biosynthesis,
pubmed-meshheading:14612452-Protein Structure, Tertiary,
pubmed-meshheading:14612452-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:14612452-Time Factors,
pubmed-meshheading:14612452-Transcription, Genetic,
pubmed-meshheading:14612452-Transfection,
pubmed-meshheading:14612452-Two-Hybrid System Techniques
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pubmed:year |
2004
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pubmed:articleTitle |
CENP-B interacts with CENP-C domains containing Mif2 regions responsible for centromere localization.
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pubmed:affiliation |
Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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