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Vol. 12, No. 9, pp. 1338-1347, May 1, 1998
1 Laboratory of Molecular Biology, National Cancer
Institute, Bethesda, Maryland 20892 USA;
2 Department of
Biology, Massachusetts Institute of Technology,
Cambridge, Masaschusetts 02139 USA
Interruption of translation in Escherichia coli can lead
to the addition of an 11-residue carboxy-terminal peptide tail to the
nascent chain. This modification is mediated by SsrA RNA (also called
10Sa RNA and tmRNA) and marks the tagged polypeptide for proteolysis.
Degradation in vivo of 
repressor amino-terminal domain variants
bearing this carboxy-terminal SsrA peptide tag is shown here to depend
on the cytoplasmic proteases ClpXP and ClpAP. Degradation in vitro of
SsrA-tagged substrates was reproduced with purified components and
required a substrate with a wild-type SsrA tail, the presence of both
ClpP and either ClpA or ClpX, and ATP. Clp-dependent proteolysis
accounts for most degradation of SsrA-tagged amino-domain substrates at
32°C, but additional proteases contribute to the degradation of some
of these SsrA-tagged substrates at 39°C. The existence of multiple
cytoplasmic proteases that function in SsrA quality-control
surveillance suggests that the SsrA tag is designed to serve as a
relatively promiscuous signal for proteolysis. Having diverse
degradation systems able to recognize this tag may increase degradation
capacity, permit degradation of a wide variety of different tagged
proteins, or allow SsrA-tagged proteins to be degraded under different
growth conditions.
[Key Words:
10Sa RNA; repressor; Escherichia
coli; intracellular proteolysis; molecular recognition; ATP-dependent
degradation]
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