Mutations in the C-terminal fragment of DnaK affecting peptide binding.

Abstract:

:Escherichia coli DnaK acts as a molecular chaperone through its ATP-regulated binding and release of polypeptide substrates. Overexpressing a C-terminal fragment (CTF) of DnaK (Gly-384 to Lys-638) containing the polypeptide substrate binding domain is lethal in wild-type E. coli. This dominant-negative phenotype may result from the nonproductive binding of CTF to cellular polypeptide targets of DnaK. Mutations affecting DnaK substrate binding were identified by selecting noncytotoxic CTF mutants followed by in vitro screening. The clustering of such mutations in the three-dimensional structure of CTF suggests the model that loops L1,2 and L4,5 form a rigid core structure critical for interactions with substrate.

authors

Burkholder WF,Zhao X,Zhu X,Hendrickson WA,Gragerov A,Gottesman ME

doi

10.1073/pnas.93.20.10632

subject

Has Abstract

pub_date

1996-10-01 00:00:00

pages

10632-7

issue

20

eissn

0027-8424

issn

1091-6490

journal_volume

93

pub_type

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