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PMID: 14532007 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Differential contributions of condensin I and condensin II to mitotic chromosome architecture in vertebrate cells.

Cell ·Vol. 115 ·No. 1 ·2003-10-03 ·Pages 109-21

Ono T, Losada A, Hirano M, Myers MP, Neuwald AF, Hirano T

Abstract

The canonical condensin complex (henceforth condensin I) plays an essential role in mitotic chromosome assembly and segregation from yeast to humans. We report here the identification of a second condensin complex (condensin II) from vertebrate cells. Condensins I and II share the same pair of structural maintenance of chromosomes (SMC) subunits but contain different sets of non-SMC subunits. siRNA-mediated depletion of condensin I- or condensin II-specific subunits in HeLa cells produces a distinct, highly characteristic defect in chromosome morphology. Simultaneous depletion of both complexes causes the severest defect. In Xenopus egg extracts, condensin I function is predominant, but lack of condensin II results in the formation of irregularly shaped chromosomes. Condensins I and II show different distributions along the axis of chromosomes assembled in vivo and in vitro. We propose that the two condensin complexes make distinct mechanistic contributions to mitotic chromosome architecture in vertebrate cells.

MeSH Terms
Adenosine Triphosphatases/genetics,metabolism Animals Chromosomes/metabolism DNA-Binding Proteins/genetics,metabolism HeLa Cells Humans Macromolecular Substances Mitosis/physiology Molecular Sequence Data Multiprotein Complexes Nuclear Proteins/genetics,metabolism Oocytes/physiology Protein Isoforms/genetics,metabolism Protein Subunits/genetics,metabolism RNA, Small Interfering/metabolism Xenopus laevis
Chemicals
DNA-Binding Proteins Macromolecular Substances Multiprotein Complexes Nuclear Proteins Protein Isoforms Protein Subunits RNA, Small Interfering condensin complexes Adenosine Triphosphatases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Ono Takao
Cold Spring Harbor Laboratory, One Bungtown Road, PO Box 100, Cold Spring Harbor, NY 11724, USA.
Losada Ana
Hirano Michiko
Myers Michael P
Neuwald Andrew F
Hirano Tatsuya
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
2003-10-03
Pages
109-21
Language
English
Region
United States
NLM ID
0413066
Subset
IM
Grants
NLM NIH HHS · R01 LM006747 · United States
NCI NIH HHS · CA45508 · United States
NIGMS NIH HHS · GM53926 · United States
NLM NIH HHS · LM06747 · United States
Databases
GENBANK
AY353253
Corrections
CommentIn
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