 |
PDBsum entry 4z0u
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase/peptide
|
PDB id
|
|
|
|
4z0u
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Interaction with single-Stranded DNA-Binding protein stimulates escherichia coli ribonuclease hi enzymatic activity.
|
|
|
Authors
|
|
C.Petzold,
A.H.Marceau,
K.H.Miller,
S.Marqusee,
J.L.Keck.
|
|
|
Ref.
|
|
J Biol Chem, 2015,
290,
14626-14636.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
Single-stranded (ss) DNA-binding proteins (SSBs) bind and protect ssDNA
intermediates formed during replication, recombination, and repair reactions.
SSBs also directly interact with many different genome maintenance proteins to
stimulate their enzymatic activities and/or mediate their proper cellular
localization. We have identified an interaction formed between Escherichia coli
SSB and ribonuclease HI (RNase HI), an enzyme that hydrolyzes RNA in RNA/DNA
hybrids. The RNase HI·SSB complex forms by RNase HI binding the intrinsically
disordered C terminus of SSB (SSB-Ct), a mode of interaction that is shared
among all SSB interaction partners examined to date. Residues that comprise the
SSB-Ct binding site are conserved among bacterial RNase HI enzymes, suggesting
that RNase HI·SSB complexes are present in many bacterial species and that
retaining the interaction is important for its cellular function. A steady-state
kinetic analysis shows that interaction with SSB stimulates RNase HI activity by
lowering the reaction Km. SSB or RNase HI protein variants that disrupt complex
formation nullify this effect. Collectively our findings identify a direct RNase
HI/SSB interaction that could play a role in targeting RNase HI activity to
RNA/DNA hybrid substrates within the genome.
|
|
|
|
|
|
|
