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J. Biol. Chem., Vol. 278, Issue 5, 3314-3322, January 31, 2003
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From the Laboratory of Biochemistry, School of Medicine, University
of Patras, 26110 Patras, Greece and § Department of
Chemistry & Environmental Technology, Kinki University,
Hiroshima 739-2116, Japan
Yeast ribosomal protein L41 is dispensable in the
yeast. Its absence had no effect on polyphenylalanine synthesis
activity, and a limited effect on growth, translational accuracy, or
the resistance toward the antibiotic paromomycin. Removal of L41 did not affect the 60:40 S ratio, but it reduced the amount of 80 S,
suggesting that L41 is involved in ribosomal subunit association. However, the two most important effects of L41 were on
peptidyltransferase activity and translocation. Peptidyltransferase
activity was measured as a second-order rate constant
(kcat/Ks) corresponding to
the rate of peptide bond formation; this
kcat/Ks was lowered 3-fold
to 1.15 min
A Dispensable Yeast Ribosomal Protein Optimizes
Peptidyltransferase Activity and Affects Translocation*
,
1 mM1 in the L41
mutant compared with 3.46 min1
mM1 in the wild type. Translocation was also
affected by L41. Elongation factor 2 (EF2)-dependent
(enzymatic) translocation of Ac-Phe-tRNA from the A- to P-site was more
efficient in the absence of L41, because 50% translocation was
achieved at only 0.004 µM EF2 compared with 0.02 µM for the wild type. Furthermore, the
EF2-dependent translocation was inhibited by 50% at 2.5 µM of the translocation inhibitor cycloheximide in the
L41 mutant compared with 1.2 µM in the wild type.
Finally, the rate of EF2-independent (spontaneous) translocation was
increased in the absence of L41.
*
This work was supported in part by a grant from the General
Secretariat of Research and Technology, Ministry of Development of
Greece (624/PENED01) to Dennis Synetos and Human Frontier Science Program Grant RG-360/93 (to K. S.).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.
Recipient of a 3-year scholarship by the Greek State Foundation of
Scholarships. Current address: Dept. of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637.
¶
To whom correspondence should be addressed. Tel.:
302610-996125; Fax: 302610-997690; E-mail:
dsynetos@med.upatras.gr.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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