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            <title xml:lang="en">Coexpression of Escherichia coli obgE, Encoding the Evolutionarily Conserved Obg GTPase, with Ribosomal Proteins L21 and L27.</title>
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                <forename type="first">Rim</forename>
                <surname>Maouche</surname>
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                <forename type="first">Hector L</forename>
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            <idno type="stamp" n="LISM-AMU">Laboratoire d'ingénierie des systèmes macromoléculaires</idno>
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                <title xml:lang="en">Coexpression of Escherichia coli obgE, Encoding the Evolutionarily Conserved Obg GTPase, with Ribosomal Proteins L21 and L27.</title>
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                <title level="j">Journal of Bacteriology</title>
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                  <publisher>American Society for Microbiology</publisher>
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              <p>Multiple essential small GTPases are involved in the assembly of the ribosome or in the control of its activity. Among them, ObgE (CgtA) has been shown recently to act as a ribosome antiassociation factor that binds to ppGpp, a regulator whose best-known target is RNA polymerase. The present study was aimed at elucidating the expression of obgE in Escherichia coli We show that obgE is cotranscribed with ribosomal protein genes rplU and rpmA and with a gene of unknown function, yhbE We show here that about 75% of the transcripts terminate before obgE, because there is a transcriptional terminator between rpmA and yhbE As expected for ribosomal protein operons, expression was highest during exponential growth, decreased during entry into stationary phase, and became almost undetectable thereafter. Expression of the operon was derepressed in mutants lacking ppGpp or DksA. However, regulation by these factors appears to occur post-transcription initiation, since no effects of ppGpp and DksA on rplU promoter activity were observed in vitro</p>
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