Y Maki1, H Yoshida, A Wada. 1. Japan Science and Technology Corporation, Kawaguchi, Saitama 332-0012, Japan. ymaki@art.osaka-med.ac.jp
Abstract
BACKGROUND: Ribosomes in Escherichia coli change their composition and conformation in the stationary phase. Ribosome modulation factor (RMF) and ribosomal protein S22 are known to be associated with stationary phase ribosomes. RMF association causes the loss of translational activity and the dimerization of 70S ribosomes into 100S ribosomes, which may increase cell survival in the stationary phase. RESULTS: Two weakly acidic proteins having related amino acid sequences were found to be associated with E. coli ribosomes in the stationary phase. These proteins are the products of ORFs named yfiA and yhbH. The sum of the copy numbers of their product proteins, YfiA and YhbH, in the ribosomal particles was low in the log phase, but increased to nearly one in the stationary phase. YfiA was found in the 70S ribosomal fraction rather than the 100S. On the other hand, YhbH was detected exclusively in the 100S ribosomal fraction. When the stationary phase cells were transferred to fresh medium, YfiA and YhbH were found in the 70S ribosomal fraction, but not in the polysome fraction. CONCLUSIONS: Two proteins, YfiA and YhbH, associated with E. coli ribosomes were found to accumulate in the stationary phase, leading to the formation of several types of ribosomes. They are not likely to have roles in the elongation step of the translation in log phase cells, but are likely to be involved in the stabilization and preservation of ribosomes in the stationary phase, which might be necessary for cell survival.
BACKGROUND: Ribosomes in Escherichia coli change their composition and conformation in the stationary phase. Ribosome modulation factor (RMF) and ribosomal protein S22 are known to be associated with stationary phase ribosomes. RMF association causes the loss of translational activity and the dimerization of 70S ribosomes into 100S ribosomes, which may increase cell survival in the stationary phase. RESULTS: Two weakly acidic proteins having related amino acid sequences were found to be associated with E. coli ribosomes in the stationary phase. These proteins are the products of ORFs named yfiA and yhbH. The sum of the copy numbers of their product proteins, YfiA and YhbH, in the ribosomal particles was low in the log phase, but increased to nearly one in the stationary phase. YfiA was found in the 70S ribosomal fraction rather than the 100S. On the other hand, YhbH was detected exclusively in the 100S ribosomal fraction. When the stationary phase cells were transferred to fresh medium, YfiA and YhbH were found in the 70S ribosomal fraction, but not in the polysome fraction. CONCLUSIONS: Two proteins, YfiA and YhbH, associated with E. coli ribosomes were found to accumulate in the stationary phase, leading to the formation of several types of ribosomes. They are not likely to have roles in the elongation step of the translation in log phase cells, but are likely to be involved in the stabilization and preservation of ribosomes in the stationary phase, which might be necessary for cell survival.
Authors: Manjuli R Sharma; Alexandra Dönhöfer; Chandana Barat; Viter Marquez; Partha P Datta; Paola Fucini; Daniel N Wilson; Rajendra K Agrawal Journal: J Biol Chem Date: 2009-12-04 Impact factor: 5.157
Authors: Dawid Krokowski; Francesca Gaccioli; Mithu Majumder; Michael R Mullins; Celvie L Yuan; Barbara Papadopoulou; William C Merrick; Anton A Komar; Derek Taylor; Maria Hatzoglou Journal: Cell Cycle Date: 2011-08-15 Impact factor: 4.534
Authors: Julio O Ortiz; Florian Brandt; Valério R F Matias; Lau Sennels; Juri Rappsilber; Sjors H W Scheres; Matthias Eibauer; F Ulrich Hartl; Wolfgang Baumeister Journal: J Cell Biol Date: 2010-08-23 Impact factor: 10.539