Snm1B interacts with PSF2.

Snm1B interacts with PSF2.

The protein Snm1B plays a key role in interstrand crosslink (ICL) repair. In a yeast two-hybrid screen we identified the protein PSF2 to bind Snm1B. PSF2 is a member of the GINS complex involved in replication initiation and elongation, and is known to play a role in ICL repair. Snm1B was shown to b...

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Autores principales: Jay R Stringer, Christopher M Counter
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2012
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Acceso en línea:https://doaj.org/article/949362cf215a49f8b31ccfd33387827d
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spelling oai:doaj.org-article:949362cf215a49f8b31ccfd33387827d2021-11-18T08:07:38ZSnm1B interacts with PSF2.1932-620310.1371/journal.pone.0049626https://doaj.org/article/949362cf215a49f8b31ccfd33387827d2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23189151/?tool=EBIhttps://doaj.org/toc/1932-6203The protein Snm1B plays a key role in interstrand crosslink (ICL) repair. In a yeast two-hybrid screen we identified the protein PSF2 to bind Snm1B. PSF2 is a member of the GINS complex involved in replication initiation and elongation, and is known to play a role in ICL repair. Snm1B was shown to bind PSF2 in human cells through two regions, strongly to a 144 amino acid N-terminal region and weakly to a second smaller 37 amino acid C-terminal region. Ectopic expression of PSF2 increased the amount of Mus81, a protein component of the endonucleolytic complex involved in ICL repair, co-immunoprecipitating with Snm1B. Moreover, deleting the N-terminal, but not C-terminal region of Snm1B reduced the amount of co-immunoprecipitated Mus81. Conversely, the telomere-binding protein TRF2 competed with PSF2 for binding to the C-terminus of Snm1B, and deletion of this region, but not the N-terminal region, reduced Snm1B chromatin association. We speculate that the N-terminal region of Snm1B forms a complex containing PSF2 and Mus81, while the C-terminal region is important for PSF2-mediated chromatin association.Jay R StringerChristopher M CounterPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 11, p e49626 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Jay R Stringer
Christopher M Counter
Snm1B interacts with PSF2.
description The protein Snm1B plays a key role in interstrand crosslink (ICL) repair. In a yeast two-hybrid screen we identified the protein PSF2 to bind Snm1B. PSF2 is a member of the GINS complex involved in replication initiation and elongation, and is known to play a role in ICL repair. Snm1B was shown to bind PSF2 in human cells through two regions, strongly to a 144 amino acid N-terminal region and weakly to a second smaller 37 amino acid C-terminal region. Ectopic expression of PSF2 increased the amount of Mus81, a protein component of the endonucleolytic complex involved in ICL repair, co-immunoprecipitating with Snm1B. Moreover, deleting the N-terminal, but not C-terminal region of Snm1B reduced the amount of co-immunoprecipitated Mus81. Conversely, the telomere-binding protein TRF2 competed with PSF2 for binding to the C-terminus of Snm1B, and deletion of this region, but not the N-terminal region, reduced Snm1B chromatin association. We speculate that the N-terminal region of Snm1B forms a complex containing PSF2 and Mus81, while the C-terminal region is important for PSF2-mediated chromatin association.
format article
author Jay R Stringer
Christopher M Counter
author_facet Jay R Stringer
Christopher M Counter
author_sort Jay R Stringer
title Snm1B interacts with PSF2.
title_short Snm1B interacts with PSF2.
title_full Snm1B interacts with PSF2.
title_fullStr Snm1B interacts with PSF2.
title_full_unstemmed Snm1B interacts with PSF2.
title_sort snm1b interacts with psf2.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/949362cf215a49f8b31ccfd33387827d
work_keys_str_mv AT jayrstringer snm1binteractswithpsf2
AT christophermcounter snm1binteractswithpsf2
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