MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
about
The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldariusGenome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the ArchaeaCrystal structure of the NurA-dAMP-Mn2+ complexStructural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complexEnd-resection at DNA double-strand breaks in the three domains of lifeEfficient 5'-3' DNA end resection by HerA and NurA is essential for cell viability in the crenarchaeon Sulfolobus islandicusComparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packagingNanobiomotors of archaeal DNA repair machineries: current research status and application potentialLinked domain architectures allow for specialization of function in the FtsK/SpoIIIE ATPases of ESX secretion systemsBiochemical and Functional Characterization of the NurA-HerA Complex from Deinococcus radiodurans.Development of a simvastatin selection marker for a hyperthermophilic acidophile, Sulfolobus islandicus.NurA Is Endowed with Endo- and Exonuclease Activities that Are Modulated by HerA: New Insight into Their Role in DNA-End ProcessingA Novel C-Terminal Domain of RecJ is Critical for Interaction with HerA in Deinococcus radioduransRad50 is not essential for the Mre11-dependent repair of DNA double-strand breaks in Halobacterium sp. strain NRC-1.Archaeal genome guardians give insights into eukaryotic DNA replication and damage response proteins.Structural studies of DNA end detection and resection in homologous recombination.Redox stress proteins are involved in adaptation response of the hyperthermoacidophilic archaeon Sulfolobus solfataricus to nickel challenge.Molecular architecture of the HerA-NurA DNA double-strand break resection complex.Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA double-strand break.The carboxyl terminal of the archaeal nuclease NurA is involved in the interaction with single-stranded DNA-binding protein and dimer formation.Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex.Resistance to UV Irradiation Caused by Inactivation of and Genes in Thermus thermophilus
P2860
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P2860
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
description
2004 nî lūn-bûn
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2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@ast
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@en
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@nl
type
label
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@ast
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@en
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@nl
prefLabel
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@ast
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@en
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@nl
P2093
P2860
P356
P1433
P1476
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
@en
P2093
Angelo Manzan
Cara E Lang
Günter Pfeiffer
James P Carney
Melissa L Hefferin
P2860
P356
10.1038/SJ.EMBOR.7400037
P577
2004-01-01T00:00:00Z