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hSSB1 and hSSB2 Form Similar Multiprotein Complexes That Participate in DNA Damage Response
hSSB1 (human single strand DNA-binding protein 1) has been shown to participate in homologous recombination (HR)-dependent repair of DNA double strand breaks (DSBs) and ataxia telangiectasia-mutated (ATM)-mediated checkpoint pathways. Here we present evidence that hSSB2, a homolog of hSSB1, plays a...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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American Society for Biochemistry and Molecular Biology
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2749126/ https://www.ncbi.nlm.nih.gov/pubmed/19605351 http://dx.doi.org/10.1074/jbc.C109.039586 |
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author | Li, Yongjiang Bolderson, Emma Kumar, Rakesh Muniandy, Parameswary A. Xue, Yutong Richard, Derek J. Seidman, Michael Pandita, Tej K. Khanna, Kum Kum Wang, Weidong |
author_facet | Li, Yongjiang Bolderson, Emma Kumar, Rakesh Muniandy, Parameswary A. Xue, Yutong Richard, Derek J. Seidman, Michael Pandita, Tej K. Khanna, Kum Kum Wang, Weidong |
author_sort | Li, Yongjiang |
collection | PubMed |
description | hSSB1 (human single strand DNA-binding protein 1) has been shown to participate in homologous recombination (HR)-dependent repair of DNA double strand breaks (DSBs) and ataxia telangiectasia-mutated (ATM)-mediated checkpoint pathways. Here we present evidence that hSSB2, a homolog of hSSB1, plays a role similar to hSSB1 in DNA damage-response pathways. This was evidenced by findings that hSSB2-depleted cells resemble hSSB1-depleted cells in hypersensitivity to DNA-damaging reagents, reduced efficiency in HR-dependent repair of DSBs, and defective ATM-dependent phosphorylation. Notably, hSSB1 and hSSB2 form separate complexes with two identical proteins, INTS3 and hSSBIP1 (C9ORF80). Cells depleted of INTS3 and hSSBIP1 also exhibited hypersensitivity to DNA damage reagents, chromosomal instability, and reduced ATM-dependent phosphorylation. hSSBIP1 was rapidly recruited to laser-induced DSBs, a feature also similar to that reported for hSSB1. Depletion of INTS3 decreased the stability of hSSB1 and hSSBIP1, suggesting that INTS3 may provide a scaffold to allow proper assembly of the hSSB complexes. Thus, our data demonstrate that hSSB1 and hSSB2 form two separate complexes with similar structures, and both are required for efficient HR-dependent repair of DSBs and ATM-dependent signaling pathways. |
format | Text |
id | pubmed-2749126 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-27491262009-09-25 hSSB1 and hSSB2 Form Similar Multiprotein Complexes That Participate in DNA Damage Response Li, Yongjiang Bolderson, Emma Kumar, Rakesh Muniandy, Parameswary A. Xue, Yutong Richard, Derek J. Seidman, Michael Pandita, Tej K. Khanna, Kum Kum Wang, Weidong J Biol Chem DNA: Replication, Repair, Recombination, and Chromosome Dynamics hSSB1 (human single strand DNA-binding protein 1) has been shown to participate in homologous recombination (HR)-dependent repair of DNA double strand breaks (DSBs) and ataxia telangiectasia-mutated (ATM)-mediated checkpoint pathways. Here we present evidence that hSSB2, a homolog of hSSB1, plays a role similar to hSSB1 in DNA damage-response pathways. This was evidenced by findings that hSSB2-depleted cells resemble hSSB1-depleted cells in hypersensitivity to DNA-damaging reagents, reduced efficiency in HR-dependent repair of DSBs, and defective ATM-dependent phosphorylation. Notably, hSSB1 and hSSB2 form separate complexes with two identical proteins, INTS3 and hSSBIP1 (C9ORF80). Cells depleted of INTS3 and hSSBIP1 also exhibited hypersensitivity to DNA damage reagents, chromosomal instability, and reduced ATM-dependent phosphorylation. hSSBIP1 was rapidly recruited to laser-induced DSBs, a feature also similar to that reported for hSSB1. Depletion of INTS3 decreased the stability of hSSB1 and hSSBIP1, suggesting that INTS3 may provide a scaffold to allow proper assembly of the hSSB complexes. Thus, our data demonstrate that hSSB1 and hSSB2 form two separate complexes with similar structures, and both are required for efficient HR-dependent repair of DSBs and ATM-dependent signaling pathways. American Society for Biochemistry and Molecular Biology 2009-08-28 2009-07-14 /pmc/articles/PMC2749126/ /pubmed/19605351 http://dx.doi.org/10.1074/jbc.C109.039586 Text en © 2009 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles |
spellingShingle | DNA: Replication, Repair, Recombination, and Chromosome Dynamics Li, Yongjiang Bolderson, Emma Kumar, Rakesh Muniandy, Parameswary A. Xue, Yutong Richard, Derek J. Seidman, Michael Pandita, Tej K. Khanna, Kum Kum Wang, Weidong hSSB1 and hSSB2 Form Similar Multiprotein Complexes That Participate in DNA Damage Response |
title | hSSB1 and hSSB2 Form Similar Multiprotein Complexes That Participate in DNA Damage Response |
title_full | hSSB1 and hSSB2 Form Similar Multiprotein Complexes That Participate in DNA Damage Response |
title_fullStr | hSSB1 and hSSB2 Form Similar Multiprotein Complexes That Participate in DNA Damage Response |
title_full_unstemmed | hSSB1 and hSSB2 Form Similar Multiprotein Complexes That Participate in DNA Damage Response |
title_short | hSSB1 and hSSB2 Form Similar Multiprotein Complexes That Participate in DNA Damage Response |
title_sort | hssb1 and hssb2 form similar multiprotein complexes that participate in dna damage response |
topic | DNA: Replication, Repair, Recombination, and Chromosome Dynamics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2749126/ https://www.ncbi.nlm.nih.gov/pubmed/19605351 http://dx.doi.org/10.1074/jbc.C109.039586 |
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