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Identification of an mRNA element promoting rate‐limiting cleavage of the polycistronic puf mRNA in Rhodobacter capsulatus by an enzyme to RNase E
Author(s) -
Fritsch Jürgen,
Rothfuchs Rüdiger,
Rauhut Reinhard,
Klug Gabrrele
Publication year - 1995
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1995.tb02277.x
Subject(s) - endoribonuclease , rhodobacter , biology , rnase h , rnase p , degradosome , messenger rna , microbiology and biotechnology , escherichia coli , ribonuclease iii , rna , biochemistry , gene , mutant , rna interference
Summary We have identified an mRNA element that is involved in the initial cleavage of the pufBALMX mRNA species in Rhodobacter capsulatus. This endoribonuclease recognition site, the first to be identified in a bacterial species other than Escherichia coli , shows strong similarities to mRNA sequences cleaved by the endoribonuclease E in E. coli. The presence of an RNase E‐like enzyme in R capsulatus is further supported by in vitro cleavage of E. coli transcripts by R. capsulatus extracts at sites attributed to RNase E and by the cross‐reaction of a polypeptide from R capsulatus with antisera against E. coli RNase E. Our data provide evidence that mRNAs are degraded in different bacterial species by enzymes with similar recognition sequences and activities. We present a model that attributes the segmental differences in stability of the polycistronic puf transcript to a specific distribution of mRNA decay‐promoting and mRNA decay‐impeding elements.