title: Two proteins, YfiA and YhbH, associated with resting ribosomes in stationary phase Escherichia coli.
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.
authors.affiliation: Japan Science and Technology Corporation, Kawaguchi, Saitama 332-0012, Japan. ymaki@art.osaka-med.ac.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Maki
authors.forename: H
authors.initials: H
authors.lastname: Yoshida
authors.forename: A
authors.initials: A
authors.lastname: Wada
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D003470:Culture Media; D004926:Escherichia coli / Q000254:growth & development* / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008969:Molecular Sequence Data; D011485:Protein Binding; D012269:Ribosomal Proteins / Q000302:isolation & purification / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism* / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media; D029968:Escherichia coli Proteins; C422854:HPF protein, E coli; C434525:RaiA protein, E coli; D012269:Ribosomal Proteins; C499682:YfiA protein, bacteria