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Two proteins, YfiA and YhbH, associated with resting ribosomes in stationary phase Escherichia coli by Yasushi Maki; Hideji Yoshida; Akira Wada is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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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. 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. Two proteins, YfiA and YhbH, associated with __E. coli__ ribosomes were found to accumulate in the stationary pha

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Author

Yasushi Maki; Hideji Yoshida; Akira Wada

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 1356-9597)

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)