MULTIPLE DEGRADATION PATHWAYS OF THE RPSO MESSENGER-RNA OF ESCHERICHIA-COLI - RNASE-E INTERACTS WITH THE 5'-EXTREMITIES AND 3'-EXTREMITIES OF THE PRIMARY TRANSCRIPT
E. Hajnsdorf et al., MULTIPLE DEGRADATION PATHWAYS OF THE RPSO MESSENGER-RNA OF ESCHERICHIA-COLI - RNASE-E INTERACTS WITH THE 5'-EXTREMITIES AND 3'-EXTREMITIES OF THE PRIMARY TRANSCRIPT, Biochimie, 78(6), 1996, pp. 416-424
The degradation process of the rpsO mRNA is one of the best characteri
sed in E coli. Two independent degradation pathways have been identifi
ed. The first one is initiated by an RNase E endonucleolytic cleavage
which allows access to the transcript by polynucleotide phosphorylase
and RNase II. Cleavage by RNase E gives rise to an rpsO message lackin
g the stabilising hairpin of the primary transcript; this truncated mR
NA is then degraded exonucleolytically from its 3' terminus. This path
way might be coupled to the translation of the message. The second pat
hway allows degradation of polyadenylated rpsO mRNA independently of R
Nase II, PNPase and RNase E. The ribonucleases responsible for degrada
tion of poly(A) mRNAs under these conditions are not known. Poly(A) ta
ils have been proposed to facilitate the degradation of structured RNA
by polynucleotide phosphorylase. In contrast, we believe that removal
of poly(A) by RNase II stabilises the rpsO mRNA harbouring a 3' hairp
in. In addition to these two pathways, we have identified endonucleoly
tic cleavages which occur only in strains deficient for both RNase E a
nd RNase III suggesting that these two endonucleases protect the 5' le
ader of the mRNA from the attack of unidentified ribonuclease(s). Loop
ing of the rpsO mRNA might explain how RNase E bound at the 5' end can
cleave at a site located just upstream the hairpin of the transcripti
on terminator.