Probing the ATP-binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis
نویسندگان
چکیده
منابع مشابه
Modulation of the P1 plasmid partition protein ParA by ATP, ADP, and P1 ParB.
ParA is an essential P1 plasmid partition protein. It represses transcription of the par genes (parA and parB) and is also required for a second, as yet undefined step in partition. ParA is a ParB-stimulated ATPase that binds to a specific DNA site in the par promoter region. ATP binding and hydrolysis by ParA affect ParA activities in vitro. ATP and ADP binding stimulate ParA DNA binding and d...
متن کاملP1 ParA interacts with the P1 partition complex at parS and an ATP-ADP switch controls ParA activities.
The partition system of P1 plasmids is composed of two proteins, ParA and ParB, and a cis-acting site parS. parS is wrapped around ParB and Escherichia coli IHF protein in a higher order nucleoprotein complex called the partition complex. ParA is an ATPase that autoregulates the expression of the par operon and has an essential but unknown function in the partition process. In this study we dem...
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A protonated Zn(II) complex with a terpyridine-containing pentaamine macrocycle catalyses ATP hydrolysis in the presence of a second metal ion, which acts as cofactor assisting the phosphoryl transfer from ATP to an amine group of the receptor.
متن کاملATP-regulated interactions between P1 ParA, ParB and non-specific DNA that are stabilized by the plasmid partition site, parS
Localization of the P1 plasmid requires two proteins, ParA and ParB, which act on the plasmid partition site, parS. ParB is a site-specific DNA-binding protein and ParA is a Walker-type ATPase with non-specific DNA-binding activity. In vivo ParA binds the bacterial nucleoid and forms dynamic patterns that are governed by the ParB-parS partition complex on the plasmid. How these interactions dri...
متن کاملATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome.
The 26S proteasome degrades polyubiquitinated proteins by an energy-dependent mechanism. Here we define multiple roles for ATP in 26S proteasome function. ATP binding is necessary and sufficient for assembly of 26S proteasome from 20S proteasome and PA700/19S subcomplexes and for proteasome activation. Proteasome assembly and activation may require distinct ATP binding events. The 26S proteasom...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2001
ISSN: 1460-2075
DOI: 10.1093/emboj/20.17.4901