Characterization of the Interaction between the Cohesin Subunits Rad21 and SA1/2

Simple item page
dc.citation.firstpagee69458
dc.citation.issueNumber7
dc.citation.journalTitlePLoS One
dc.citation.volumeNumber8
dc.contributor.authorZhang, Nenggang
dc.contributor.authorJiang, Yunyun
dc.contributor.authorMao, Qilong
dc.contributor.authorDemeler, Borries
dc.contributor.authorTao, Yizhi Jane
dc.contributor.authorPati, Debananda
dc.date.accessioned2013-07-19T15:38:07Z
dc.date.available2013-07-19T15:38:07Z
dc.date.issued2013
dc.description.abstractThe cohesin complex is responsible for the fidelity of chromosomal segregation during mitosis. It consists of four core subunits, namely Rad21/Mcd1/Scc1, Smc1, Smc3, and one of the yeast Scc3 orthologs SA1 or SA2. Sister chromatid cohesion is generated during DNA replication and maintained until the onset of anaphase. Among the many proposed models of the cohesin complex, the ﾒcoreﾒ cohesin subunits Smc1, Smc3, and Rad21 are almost universally displayed as tripartite ring. However, other than its supportive role in the cohesin ring, little is known about the fourth core subunit SA1/SA2. To gain deeper insight into the function of SA1/SA2 in the cohesin complex, we have mapped the interactive regions of SA2 and Rad21 in vitro and ex vivo. Whereas SA2 interacts with Rad21 through a broad region (301ﾖ750 aa), Rad21 binds to SA proteins through two SA-binding motifs on Rad21, namely N-terminal (NT) and middle part (MP) SA-binding motif, located At 60-81 aa of the N-terminus and 383ﾖ392 aa of the MP of Rad21, respectively. The MP SA-binding motif is a 10 amino acid, a-helical motif. Deletion of these 10 amino acids or mutation of three conserved amino acids (L385, F389, and T390) in this ahelical motif significantly hinders Rad21 from physically interacting with SA1/2. Besides the MP SA-binding motif, the NT SAbinding motif is also important for SA1/2 interaction. Although mutations on both SA-binding motifs disrupt Rad21-SA1/2 interaction, they had no apparent effect on the Smc1-Smc3-Rad21 interaction. However, the Rad21-Rad21 dimerization was reduced by the mutations, indicating potential involvement of the two SA-binding motifs in the formation of the two-ring handcuff for chromosomal cohesion. Furthermore, mutant Rad21 proteins failed to significantly rescue precocious chromosome separation caused by depletion of endogenous Rad21 in mitotic cells, further indicating the physiological significance of the two SA-binding motifs of Rad21.
dc.embargo.termsnone
dc.identifier.citationZhang, Nenggang, Jiang, Yunyun, Mao, Qilong, et al.. "Characterization of the Interaction between the Cohesin Subunits Rad21 and SA1/2." <i>PLoS One,</i> 8, no. 7 (2013) Public Library of Science: e69458. http://dx.doi.org/10.1371/journal.pone.0069458.
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0069458
dc.identifier.urihttps://hdl.handle.net/1911/71602
dc.language.isoeng
dc.publisherPublic Library of Science
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.titleCharacterization of the Interaction between the Cohesin Subunits Rad21 and SA1/2
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpublisher version
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
CharacterizationInteraction.pdf
Size:
5.59 MB
Format:
Adobe Portable Document Format
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.61 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Biochemistry and Cell Biology Publications
Faculty Publications