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Regulation of the Rhp26ERCC6/CSB chromatin remodeler by a novel conserved leucine latch motif.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2014 Dec 30; Vol. 111 (52), pp. 18566-71. Date of Electronic Publication: 2014 Dec 15. - Publication Year :
- 2014
-
Abstract
- CSB/ERCC6 (Cockayne syndrome B protein/excision repair cross-complementation group 6), a member of a subfamily of SWI2/SNF2 (SWItch/sucrose nonfermentable)-related chromatin remodelers, plays crucial roles in gene expression and the maintenance of genome integrity. Here, we report the mechanism of the autoregulation of Rhp26, which is the homolog of CSB/ERCC6 in Schizosaccharomyces pombe. We identified a novel conserved protein motif, termed the "leucine latch," at the N terminus of Rhp26. The leucine latch motif mediates the autoinhibition of the ATPase and chromatin-remodeling activities of Rhp26 via its interaction with the core ATPase domain. Moreover, we found that the C terminus of the protein counteracts this autoinhibition and that both the N- and C-terminal regions of Rhp26 are needed for its proper function in DNA repair in vivo. The presence of the leucine latch motif in organisms ranging from yeast to humans suggests a conserved mechanism for the autoregulation of CSB/ERCC6 despite the otherwise highly divergent nature of the N- and C-terminal regions.
- Subjects :
- Amino Acid Motifs
Chromatin genetics
DNA Helicases genetics
DNA Helicases metabolism
Humans
Protein Structure, Tertiary
Schizosaccharomyces genetics
Schizosaccharomyces pombe Proteins genetics
Schizosaccharomyces pombe Proteins metabolism
Chromatin enzymology
Chromatin Assembly and Disassembly
DNA Helicases chemistry
Schizosaccharomyces enzymology
Schizosaccharomyces pombe Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1091-6490
- Volume :
- 111
- Issue :
- 52
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 25512493
- Full Text :
- https://doi.org/10.1073/pnas.1420227112