Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1998-7-29
pubmed:databankReference
pubmed:abstractText
The structural maintenance of chromosomes (SMC) family is a growing family of chromosomal ATPases. The founding class of SMC protein complexes, condensins, plays a central role in mitotic chromosome condensation. We report here a new class of SMC protein complexes containing XSMC1 and XSMC3, Xenopus homologs of yeast Smc1p and Smc3p, respectively. The protein complexes (termed cohesins) exist as two major forms with sedimentation coefficients of 9S and 14S. 9S cohesin is a heterodimer of XSMC1 and XSMC3, whereas 14S cohesin contains three additional subunits. One of them has been identified as a Xenopus homolog of the Schizosaccharomyces pombe Rad21p implicated in DNA repair and the Saccharomyces cerevisiae Scc1p/Mcd1p implicated in sister chromatid cohesion. 14S cohesin binds to interphase chromatin independently of DNA replication and dissociates from it at the onset of mitosis. Immunodepletion of cohesins during interphase causes defects in sister chromatid cohesion in subsequent mitosis, whereas condensation is unaffected. These results suggest that proper assembly of mitotic chromosomes is regulated by two distinct classes of SMC protein complexes, cohesins and condensins.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-1315785, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-1480481, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-1839804, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-1846030, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-3026636, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-3339085, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-3779837, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-3888407, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-6601299, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-7559788, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-7575493, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-7662362, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-7698648, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-7758114, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-7893122, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-7954811, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-7957061, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8276886, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8381118, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8670910, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8763828, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8812457, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8849887, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8849894, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8858148, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8861912, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8895658, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8939603, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-8970729, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-9160743, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-9285594, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-9288743, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-9335333, http://linkedlifedata.com/resource/pubmed/commentcorrection/9649503-9335334
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins, http://linkedlifedata.com/resource/pubmed/chemical/condensin complexes, http://linkedlifedata.com/resource/pubmed/chemical/structural maintenance of...
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1986-97
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:9649503-Animals, pubmed-meshheading:9649503-Adenosine Triphosphatases, pubmed-meshheading:9649503-Xenopus laevis, pubmed-meshheading:9649503-Fungal Proteins, pubmed-meshheading:9649503-Molecular Weight, pubmed-meshheading:9649503-Mitosis, pubmed-meshheading:9649503-Nuclear Envelope, pubmed-meshheading:9649503-Chromatin, pubmed-meshheading:9649503-Amino Acid Sequence, pubmed-meshheading:9649503-Macromolecular Substances, pubmed-meshheading:9649503-DNA Replication, pubmed-meshheading:9649503-Chromatids, pubmed-meshheading:9649503-Molecular Sequence Data, pubmed-meshheading:9649503-Interphase, pubmed-meshheading:9649503-Cloning, Molecular, pubmed-meshheading:9649503-Sequence Homology, Amino Acid, pubmed-meshheading:9649503-DNA-Binding Proteins, pubmed-meshheading:9649503-Chromosomal Proteins, Non-Histone, pubmed-meshheading:9649503-Multiprotein Complexes, pubmed-meshheading:9649503-Xenopus Proteins
More...