L1O Is Rapidly Degraded When Synthesized in Excess of Ribosomal Protein L7/L12
نویسنده
چکیده
In Escherichia coli the genes encoding ribosomal proteins L10 and L7/12, rpU and rplL, respectively, are cotranscribed and subject to translational coupling. Synthesis of both proteins is coordinately regulated at the translational level by binding of L10 or a complex of L10 and L7/L12 to a single target in the mRNA leader region upstream of rpU. Unexpectedly, small deletions that inactivated the ribosome-binding site of the rpIL gene carried on multicopy plasmids exerted a negative effect on expression of the upstream rpU gene. This effect could be overcome by overproduction of L7/L12 in trans from another plasmid. This apparent stimulation resulted from stabilization of the overproduced L10 protein by L7/L12, presumably because free L10, in contrast to L10 complexed with L7/L12, is subject to rapid proteolytic decay. The contribution of this decay mechanism to the regulation of the rpUL operon is evaluated.
منابع مشابه
Escherichia coli ribosomal protein L10 is rapidly degraded when synthesized in excess of ribosomal protein L7/L12.
In Escherichia coli the genes encoding ribosomal proteins L10 and L7/12, rplJ and rplL, respectively, are cotranscribed and subject to translational coupling. Synthesis of both proteins is coordinately regulated at the translational level by binding of L10 or a complex of L10 and L7/L12 to a single target in the mRNA leader region upstream of rplJ. Unexpectedly, small deletions that inactivated...
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