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Degradation of mRNA in bacteria: emergence of ubiquitous features
Author(s) -
Régnier Philippe,
Arraiano Cecília Maria
Publication year - 2000
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(200003)22:3<235::aid-bies5>3.0.co;2-2
Subject(s) - exoribonuclease , polynucleotide phosphorylase , endoribonuclease , degradosome , biology , messenger rna , exosome complex , transcription (linguistics) , microbiology and biotechnology , rna , rnase p , p bodies , biochemistry , enzyme , translation (biology) , gene , linguistics , philosophy , purine nucleoside phosphorylase , purine
The amount of a messenger RNA available for protein synthesis depends on the efficiency of its transcription and stability. The mechanisms of degradation that determine the stability of mRNAs in bacteria have been investigated extensively during the last decade and have begun to be better understood. Several endo‐ and exoribonucleases involved in the mRNA metabolism have been characterized as well as structural features of’mRNA which account for its stability have been determined. The most important recent developments have been the discovery that the degradosome—a multiprotein complex containing an endoribonuclease (RNase E), an exoribonuclease (polynucleotide phosphorylase), and a DEAD box helicase (RhlB)—has a central role in mRNA degradation and that oligo(A) tails synthesized by poly(A) polymerase facilitate the degradation of mRNAs and RNA fragments. Moreover, the phosphorylation status and the base pairing of 5′ extremities, together with 3′ secondary structures of transcriptional terminators, contribute to the stability of primary transcripts. Degradation of mRNAs can follow several independent pathways. Interestingly, poly(A) tails and multienzyme complexes also control the stability and the degradation of eukaryotic mRNAs. These discoveries have led to the development of refined models of mRNA degradation. BioEssays 22:235–244, 2000. © 2000 John Wiley & Sons, Inc.