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Residues of 14-3-3 zeta required for activation of exoenzyme S of Pseudomonas aeruginosa.

Abstract：

:Exoenzyme S (ExoS) is a mono-ADP-ribosyltransferase secreted by the opportunistic pathogen Pseudomonas aeruginosa. ExoS requires a eukaryotic factor, the 14-3-3 protein, for enzymatic activity. Here, two aspects of the activation of the ADP-ribosyltransferase activity of ExoS by 14-3-3 proteins are examined. Initial studies showed that several isoforms of 14-3-3, including beta, zeta, eta, sigma, and tau, activated ExoS with similar efficiency. This implicates a conserved structure in 14-3-3 that contributes to the interaction between 14-3-3 and ExoS. One candidate structure is the conserved amphipathic groove that mediates the 14-3-3/Raf-1 interaction. The next series of experiments examined the role of individual amino acids of the amphipathic groove of 14-3-3 zeta in ExoS activation and showed that ExoS activation required the basic residues lining the amphipathic groove of 14-3-3 zeta without extensive involvement of the hydrophobic residues. Strikingly, mutations of Val-176 of 14-3-3 zeta that disrupted its interaction with Raf-1 did not affect the binding and activation of ExoS by 14-3-3. Thus, ExoS selectively employs residues in the Raf-binding groove for its association with 14-3-3 proteins.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Zhang L,Wang H,Masters SC,Wang B,Barbieri JT,Fu H

doi

10.1021/bi991019l

subject

Has Abstract

pub_date

1999-09-14 00:00:00

pages

12159-64

issue

37

eissn

0006-2960

issn

1520-4995

pii

bi991019l

journal_volume

38

pub_type

杂志文章

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