Biochemical Characterization of Mycobacterium smegmatis RnhC (MSMEG_4305), a Bifunctional Enzyme Composed of Autonomous N-Terminal Type I RNase H and C-Terminal Acid Phosphatase Domains.
about
Division of labor among Mycobacterium smegmatis RNase H enzymes: RNase H1 activity of RnhA or RnhC is essential for growth whereas RnhB and RnhA guard against killing by hydrogen peroxide in stationary phase.DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria.R-loop induced stress response by second (p)ppGpp synthetase in Mycobacterium smegmatis: functional and domain interdependence.
P2860
Biochemical Characterization of Mycobacterium smegmatis RnhC (MSMEG_4305), a Bifunctional Enzyme Composed of Autonomous N-Terminal Type I RNase H and C-Terminal Acid Phosphatase Domains.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Biochemical Characterization o ...... inal Acid Phosphatase Domains.
@ast
Biochemical Characterization o ...... inal Acid Phosphatase Domains.
@en
type
label
Biochemical Characterization o ...... inal Acid Phosphatase Domains.
@ast
Biochemical Characterization o ...... inal Acid Phosphatase Domains.
@en
prefLabel
Biochemical Characterization o ...... inal Acid Phosphatase Domains.
@ast
Biochemical Characterization o ...... inal Acid Phosphatase Domains.
@en
P2860
P356
P1476
Biochemical Characterization o ...... inal Acid Phosphatase Domains.
@en
P2093
Agata Jacewicz
Stewart Shuman
P2860
P304
P356
10.1128/JB.00268-15
P407
P577
2015-05-18T00:00:00Z