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J. Biol. Chem., Vol. 276, Issue 18, 14829-14834, May 4, 2001
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From the In vivo 32P-labeled yeast
proteins from wild type and ppz1 ppz2 phosphatase mutants
were resolved by bidimensional electrophoresis. A prominent
phosphoprotein, which in ppz mutants showed a marked shift
to acidic regions, was identified by mixed peptide sequencing as the
translation elongation factor 1B
A Role for the Ppz Ser/Thr Protein Phosphatases in the Regulation
of Translation Elongation Factor 1B
*
§,,
Departament de Bioquímica, Facultat
de Veterinària, Universitat Autònoma de Barcelona,
Bellaterra 08193, Spain and the ¶ Department of Pharmacology & Cancer Biology, Duke University Medical Center, Durham, North Carolina
27710
(formerly eEF1
). An equivalent
shift was detected in cells overexpressing HAL3, a inhibitory regulatory subunit of Ppz1. Subsequent analysis identified the conserved Ser-86 as the in vivo phosphorylatable
residue and showed that its phosphorylation was increased in
ppz cells. Pull-down experiments using a glutathione
S-transferase (GST)-EF1B fusion version allowed to
identify Ppz1 as an in vivo interacting protein. Cells
lacking Ppz display a higher tolerance to known translation inhibitors,
such as hygromycin and paromomycin, and enhanced readthrough at all
three nonsense codons, suggesting that translational fidelity might be
affected. Overexpression of a GST-EF1B fusion counteracted the
growth defect associated to high levels of Ppz1 and this effect was
essentially lost when the phosphorylatable Ser-86 is replaced by Ala.
Therefore, the Ppz phosphatases appear to regulate the phosphorylation
state of EF1B in yeast, and this may result in modification of the
translational accuracy.
*
This work was supported in part by Grant PB98-0565-C4-02 (to
J. A.), by Grants HL19242 and DK52378A (to T. H.), and by a
Joint Research Project sponsored by the Commission for Cultural,
Educational, and Scientific Exchange between the United States and
Spain (to J. A and T. H.). The generous support of Applied Biosystems
to the Haystead laboratory is acknowledged.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Tel.:
34-93-5812182; Fax: 34-93-5812006; E-mail: Joaquin.Arino@uab.es.
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