-
Something wrong with this record ?
Chromatin association of the SMC5/6 complex is dependent on binding of its NSE3 subunit to DNA
K. Zabrady, M. Adamus, L. Vondrova, C. Liao, H. Skoupilova, M. Novakova, L. Jurcisinova, A. Alt, AW. Oliver, AR. Lehmann, JJ. Palecek,
Language English Country England, Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Directory of Open Access Journals
from 2005
Free Medical Journals
from 1996
PubMed Central
from 1974
Europe PubMed Central
from 1974
Open Access Digital Library
from 1996-01-01 to 2030-12-31
Open Access Digital Library
from 1974-01-01
Open Access Digital Library
from 1996-01-01
Open Access Digital Library
from 1996-01-01
Medline Complete (EBSCOhost)
from 1996-01-01
Oxford Journals Open Access Collection
from 1996-01-01
ROAD: Directory of Open Access Scholarly Resources
from 1974
PubMed
26446992
DOI
10.1093/nar/gkv1021
Knihovny.cz E-resources
- MeSH
- Chromatin metabolism MeSH
- DNA metabolism MeSH
- Nuclear Proteins metabolism MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Cell Cycle Proteins chemistry metabolism MeSH
- Recombination, Genetic MeSH
- DNA Replication MeSH
- Schizosaccharomyces pombe Proteins metabolism MeSH
- Schizosaccharomyces genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Protein Binding MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
SMC5/6 is a highly conserved protein complex related to cohesin and condensin, which are the key components of higher-order chromatin structures. The SMC5/6 complex is essential for proliferation in yeast and is involved in replication fork stability and processing. However, the precise mechanism of action of SMC5/6 is not known. Here we present evidence that the NSE1/NSE3/NSE4 sub-complex of SMC5/6 binds to double-stranded DNA without any preference for DNA-replication/recombination intermediates. Mutations of key basic residues within the NSE1/NSE3/NSE4 DNA-binding surface reduce binding to DNA in vitro. Their introduction into the Schizosaccharomyces pombe genome results in cell death or hypersensitivity to DNA damaging agents. Chromatin immunoprecipitation analysis of the hypomorphic nse3 DNA-binding mutant shows a reduced association of fission yeast SMC5/6 with chromatin. Based on our results, we propose a model for loading of the SMC5/6 complex onto the chromatin.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc16028129
- 003
- CZ-PrNML
- 005
- 20161027115956.0
- 007
- ta
- 008
- 161005s2016 enk f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1093/nar/gkv1021 $2 doi
- 024 7_
- $a 10.1093/nar/gkv1021 $2 doi
- 035 __
- $a (PubMed)26446992
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a enk
- 100 1_
- $a Zabrady, Katerina $u Mendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic Laboratory of Functional Genomics and Proteomics, National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
- 245 10
- $a Chromatin association of the SMC5/6 complex is dependent on binding of its NSE3 subunit to DNA / $c K. Zabrady, M. Adamus, L. Vondrova, C. Liao, H. Skoupilova, M. Novakova, L. Jurcisinova, A. Alt, AW. Oliver, AR. Lehmann, JJ. Palecek,
- 520 9_
- $a SMC5/6 is a highly conserved protein complex related to cohesin and condensin, which are the key components of higher-order chromatin structures. The SMC5/6 complex is essential for proliferation in yeast and is involved in replication fork stability and processing. However, the precise mechanism of action of SMC5/6 is not known. Here we present evidence that the NSE1/NSE3/NSE4 sub-complex of SMC5/6 binds to double-stranded DNA without any preference for DNA-replication/recombination intermediates. Mutations of key basic residues within the NSE1/NSE3/NSE4 DNA-binding surface reduce binding to DNA in vitro. Their introduction into the Schizosaccharomyces pombe genome results in cell death or hypersensitivity to DNA damaging agents. Chromatin immunoprecipitation analysis of the hypomorphic nse3 DNA-binding mutant shows a reduced association of fission yeast SMC5/6 with chromatin. Based on our results, we propose a model for loading of the SMC5/6 complex onto the chromatin.
- 650 _2
- $a sekvence aminokyselin $7 D000595
- 650 _2
- $a proteiny buněčného cyklu $x chemie $x metabolismus $7 D018797
- 650 _2
- $a chromatin $x metabolismus $7 D002843
- 650 _2
- $a DNA $x metabolismus $7 D004247
- 650 _2
- $a replikace DNA $7 D004261
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a molekulární sekvence - údaje $7 D008969
- 650 _2
- $a jaderné proteiny $x metabolismus $7 D009687
- 650 _2
- $a vazba proteinů $7 D011485
- 650 _2
- $a rekombinace genetická $7 D011995
- 650 _2
- $a Schizosaccharomyces $x genetika $x metabolismus $7 D012568
- 650 _2
- $a Schizosaccharomyces pombe - proteiny $x metabolismus $7 D029702
- 650 _2
- $a sekvenční homologie aminokyselin $7 D017386
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Adamus, Marek $u Mendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic. $7 gn_A_00001632
- 700 1_
- $a Vondrova, Lucie $u Mendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic Laboratory of Functional Genomics and Proteomics, National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
- 700 1_
- $a Liao, Chunyan $u Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton BN1 9RQ, United Kingdom.
- 700 1_
- $a Skoupilova, Hana $u Laboratory of Functional Genomics and Proteomics, National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
- 700 1_
- $a Novakova, Marketa $u Laboratory of Functional Genomics and Proteomics, National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
- 700 1_
- $a Jurcisinova, Lenka $u Mendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic Laboratory of Functional Genomics and Proteomics, National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic.
- 700 1_
- $a Alt, Aaron $u Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton BN1 9RQ, United Kingdom. $7 gn_A_00004880
- 700 1_
- $a Oliver, Antony W $u Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton BN1 9RQ, United Kingdom.
- 700 1_
- $a Lehmann, Alan R $u Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton BN1 9RQ, United Kingdom.
- 700 1_
- $a Palecek, Jan J $u Mendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic Laboratory of Functional Genomics and Proteomics, National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kotlarska 2, Brno, 61137, Czech Republic jpalecek@sci.muni.cz.
- 773 0_
- $w MED00003554 $t Nucleic acids research $x 1362-4962 $g Roč. 44, č. 3 (2016), s. 1064-79
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/26446992 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20161005 $b ABA008
- 991 __
- $a 20161027120412 $b ABA008
- 999 __
- $a ok $b bmc $g 1166443 $s 952759
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2016 $b 44 $c 3 $d 1064-79 $e 20151007 $i 1362-4962 $m Nucleic acids research $n Nucleic Acids Res $x MED00003554
- LZP __
- $a Pubmed-20161005
