RRC ID |
30705
|
著者 |
Shimada A, Kawasoe Y, Hata Y, Takahashi TS, Masui R, Kuramitsu S, Fukui K.
|
タイトル |
MutS stimulates the endonuclease activity of MutL in an ATP-hydrolysis-dependent manner.
|
ジャーナル |
FEBS J
|
Abstract |
In the initial steps of DNA mismatch repair, MutS recognizes a mismatched base and recruits the latent endonuclease MutL onto the mismatch-containing DNA in concert with other proteins. MutL then cleaves the error-containing strand to introduce an entry point for the downstream excision reaction. Because MutL has no intrinsic ability to recognize a mismatch and discriminate between newly synthesized and template strands, the endonuclease activity of MutL is strictly regulated by ATP-binding in order to avoid nonspecific degradation of the genomic DNA. However, the activation mechanism for its endonuclease activity remains unclear. In this study, we found that the coexistence of a mismatch, ATP and MutS unlocks the ATP-binding-dependent suppression of MutL endonuclease activity. Interestingly, ATPase-deficient mutants of MutS were unable to activate MutL. Furthermore, wild-type MutS activated ATPase-deficient mutants of MutL less efficiently than wild-type MutL. We concluded that ATP hydrolysis by MutS and MutL is involved in the mismatch-dependent activation of MutL endonuclease activity.
|
巻・号 |
280(14)
|
ページ |
3467-79
|
公開日 |
2013-7-1
|
DOI |
10.1111/febs.12344
|
PMID |
23679952
|
MeSH |
Adenosine Triphosphatases / antagonists & inhibitors
Adenosine Triphosphatases / chemistry
Adenosine Triphosphatases / metabolism*
Adenosine Triphosphate / chemistry*
DNA Mismatch Repair
Enzyme Activation
Hydrolysis
Kinetics
MutS DNA Mismatch-Binding Protein / chemistry
MutS DNA Mismatch-Binding Protein / metabolism*
Plasmids / genetics
Protein Structure, Tertiary
Thermus thermophilus / enzymology*
|
IF |
4.392
|
引用数 |
13
|
WOS 分野
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
リソース情報 |
遺伝子材料 |
Thermus thermophilus expression plasmid set
TEx18D08 (THR007280)
TEx18C04 (THR007252). |