Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics

Schmiesing, John A.; Ball, Alexander R.; Gregson, Heather C.; Alderton, Janet M.; Zhou, Shi-Sheng; Yokomori, Kyoko

doi:10.1073/pnas.95.22.12906

Cited by 97 publications

(120 citation statements)

References 24 publications

Supporting

Mentioning

111

Contrasting

Order By: Relevance

“…An alternative explanation for the disappearance of most of the mSMCB-mSMCD-PW29 complex from chromosomes during mitosis is that the complex may be involved only in establishment of cohesion and not maintenance (again perhaps playing other roles throughout the cell cycle). Similar behavior has been observed for hSMC1 (Schmiesing et al, 1998) and XSMC3 (Losada et al, 1998). In our study, the proteins visualized by immunofluorescence are endogenous proteins, and the results are therefore not artefacts of transfection or overexpression.…”

Section: Discussionsupporting

confidence: 87%

“…The mechanism of this inhibition is unknown. SMC proteins are stably and stoichiometrically associated with each other (Hirano, 1998;Schmiesing et al, 1998). However, the Mcd1p, XRAD21 and probably PW29 proteins are associated with the corresponding SMC heterodimer less stably and in substoichiometric ratio and, for Mcd1p at least, in a cell-cycle-dependent fashion (Guacci et al, 1997;Losada et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, the mammalian multiprotein recombination complex RC-1 is able to catalyze renaturation of single-stranded DNA, and includes bovine homologs of XSMC1 and XSMC3 (Jessberger et al, 1996;Stursberg et al, 1999). Homologs of SMC1 and SMC3, hSMC1 and hSMC3, have also been identified in humans (Schmiesing et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Characterization of the components of the putative mammalian sister chromatid cohesion complex

Darwiche

Freeman

Strunnikov

1999

Gene

108

View full text Add to dashboard Cite

Establishing and maintaining proper sister chromatid cohesion throughout the cell cycle are essential for maintaining genome integrity. To understand how sister chromatid cohesion occurs in mammals, we have cloned and characterized mouse orthologs of proteins known to be involved in sister chromatid cohesion in other organisms. The cDNAs for the mouse orthologs of SMC1 S.c. and SMC3 S.c. , mSMCB and mSMCD respectively, were cloned and the corresponding transcripts and proteins were characterized. mSMCB and mSMCD are transcribed at similar levels in adult mouse tissues except in testis, which has an excess of mSMCD transcripts. The mSMCB and mSMCD proteins, as well as the PW29 protein, a mouse homolog of Mcd1p S.c./ Rad21 S.p. , form a complex similar to cohesin in X. laevis. mSMCB, mSMCD and PW29 protein levels show no significant cellcycle dependence. The bulk of the mSMCB, mSMCD and PW29 proteins undergo redistribution from the chromosome vicinity to the cytoplasm during prometaphase and back to the chromatin in telophase. This pattern of intracellular localization suggests a complex role for this group of SMC proteins in chromosome dynamics. The PW29 protein and PCNA, which have both been implicated in sister chromatid cohesion, do not colocalize, indicating that these proteins may not function in the same cohesion pathway. Overexpression of a PW29-GFP fusion protein in mouse fibroblasts leads to inhibition of proliferation, implicating this protein and its complex with SMC proteins in the control of mitotic cycle progression.

show abstract

Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of the components of the putative mammalian sister chromatid cohesion complex

Darwiche

Freeman

Strunnikov

1999

Gene

108

View full text Add to dashboard Cite

show abstract

“…In budding yeast Saccharomyces cerevisiae, the condensin complex is composed of five polypeptides, including the SMC heterodimer (Smc2p and Smc4p) and three non-SMC subunits (Brn1p, Ycs4p and Ycs5p/Ycg1p) (Freeman et al, 2000). Similar complexes exist in higher eukaryotes (Hirano et al, 1997;Schmiesing et al, 1998;Sutani et al, 1999;Freeman et al, 2000;Kimura et al, 2001). Dysfunction of any condensin subunit results in impaired mitotic and meiotic chromosome segregation (Strunnikov et al, 1995;Bhat et al, 1996;Freeman et al, 2000;Ouspenski et al, 2000;Hagstrom et al, 2002;Hudson et al, 2003;Ono et al, 2003;Cobbe et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Transcriptional homogenization of rDNA repeats in the episome-based nucleolus induces genome-wide changes in the chromosomal distribution of condensin

Wang

Strunnikov

2008

Plasmid

View full text Add to dashboard Cite

Condensin activity establishes and maintains mitotic chromosome condensation, however the mechanisms of condensin recognition of specific chromosomal sites remain unknown. rDNA is the chief condensin binding locus in S. cerevisiae, and the level of nucleolar transcription is one of the key factors determining condensin loading to the nucleolar organizer. A new aspect of this transcriptional control is demonstrated in cells with a diffuse (episomal) nucleolar organizer, where active transcription excludes condensin from the transcribed regions of rDNA. Genome-wide ChIPchip analysis showed that these cells acquire an altered and a more robust pattern of chromosomal condensin distribution, with increased enrichment of wild-type hotspots and with emergence of new sites, most notably in the subtelomeric regions. This genome-wide condensin relocalization induced by the increase in rDNA transcription and, possibly, nucleolar architecture uncovers a novel potential role of the nucleolus in the general chromosome organization.

show abstract

“…The composition of the condensin complex is conserved in human cells. Homologues of all five condensin subunits have been identified in the human genome and cDNAs corresponding hCAP-H, hCAP-C, hCAP-E, and the homologue of XCAP-D2, CNAP1, have been cloned (Cabello et al, 1997;Schmiesing et al, 1998;Schmiesing et al, 2000). Schmiesing et al (2000) reported that immunoprecipitation of HeLa cell extracts with CNAP1-specific antibody reveals the association with hCAP-C, hCAP-E, and two unidentified proteins corresponding to the predicted molecular weights of hCAP-H and hCAP-G. Kimura and Hirano (2001) have established the identity of these two proteins by coprecipitation of all five subunits of the 13S holocomplex from HeLa cell extracts…”

Section: Introductionmentioning

confidence: 99%

Cell Cycle-dependent Expression and Nucleolar Localization of hCAP-H

Cabello¹,

Eliseeva

He³

et al. 2001

MBoC

View full text Add to dashboard Cite

Condensin is a conserved 13S heteropentamer composed of two nonidentical structural maintenance of chromosome (SMC) family proteins, in Xenopus XCAP-C and XCAP-E, and three regulatory subunits, XCAP-D2, XCAP-G, and XCAP-H. Both biochemical and genetic analyses have demonstrated an essential role for the 13S condensin complex in mitotic chromosome condensation. Further, a potential requirement for condensin in completion of chromatid arm separation in early anaphase is demonstrated by the mutational phenotypes of the Drosophila homologues of XCAP-H, barren and XCAP-C, DmSMC4. In this study we have investigated the expression and subcellular distribution of hCAP-H, the human homolog of XCAP-H, in order to better understand its cellular functions. Transcription of hCAP-H was restricted to proliferating cells with highest expression during the G 2 phase of the cell cycle. In contrast, cellular hCAP-H protein levels were constant throughout the cell cycle. hCAP-H was found to be associated with mitotic chromosomes exhibiting a nonuniform but symmetric distribution along sister chromatids. The symmetry of hCAP-H association with sister chromatids suggests that there are sequence-dependent domains of condensin aggregation. During interphase hCAP-H, -C, and -E, have distinct punctate nucleolar localization, suggesting that condensin may associate with and modulate the conformation and function of rDNA. hCAP-H association with condensed chromatin was not observed in the early phase of chromosome condensation when histone H3 phosphorylation has already taken place. This finding is consistent with the hypothesis that histone H3 phosphorylation precedes condensin-mediated condensation.

show abstract

Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics

Cited by 97 publications

References 24 publications

Characterization of the components of the putative mammalian sister chromatid cohesion complex

Characterization of the components of the putative mammalian sister chromatid cohesion complex

Transcriptional homogenization of rDNA repeats in the episome-based nucleolus induces genome-wide changes in the chromosomal distribution of condensin

Cell Cycle-dependent Expression and Nucleolar Localization of hCAP-H

Contact Info

Product

Resources

About