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Biophys. J. BioFAST: First Published December 20, 2007. doi:10.1529/biophysj.107.121822
© 2007 by the Biophysical Society.

A more recent version of this article appeared on April 1, 2008.
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CELL BIOPHYSICS

YEAST RIBOSOMAL STALK HETEROGENEITY IN VIVO SHOWN BY TWO-PHOTON FCS AND MOLECULAR BRIGHTNESS ANALYSIS

Alberto Garcia-Marcos 1, Susana A Sanchez 2, Pilar Parada 3, John S Eid 4, David M Jameson 5, Miguel Remacha 6, Enrico Gratton 2 and Juan P.G. Ballesta 1*

1 Consejo Superior de Investigaciones Cientificas
2 University of California at Irvine
3 BioSigma S.A.
4 Pacific Biosciences
5 University of Hawaii
6 Universidad Autonoma de Madrid

* To whom correspondence should be addressed. E-mail: jpgballesta{at}cbm.uam.es.

Submitted on September 12, 2007
Revised on October 23, 2007
Accepted on 26 November 2007


  Abstract
The stalk of Saccharomyce cerevisiae ribosomes contains, on average, five distinct proteins, namely P0 and four acidic proteins P1{alpha}, P1{beta}, P2{alpha}, and P2{beta}. Each ribosome contains only one copy of P0 but the distribution of the acidic proteins among the ribosome population in vivo has not been determined. Using two-photon fluorescence correlation spectroscopy and scanning FCS, on cells expressing EGFP tagged P0, P1 and P2 proteins, we show, with brightness analysis, that individual yeast ribosomes, in vivo, are compositionally heterogeneous as regards, P1{alpha}, P1{beta}, P2{alpha}, and P2{beta}. These results are relevant to the hypothesis, based on in vitro studies, that the overall cellular pattern of expressed proteins can be determined by the distribution of the stalk proteins among the ribosome population

Key Words: Eukaryotic ribosome, Fluorescence correlation spectroscopy, Intracellular analysis, Saccharomyces cerevisiae, ribosomal phosphoproteins P0, P1, P2






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Copyright © 2007 by the Biophysical Society.