The stability of mRNA from the gsiB gene of Bacillus subtilis is dependent on the presence of a strong ribosome binding site

• DOI: 10.1007/s004380050765
• Publication Date: 2002-08-25T04:52:48Z
• Authors: B. Jürgen; T. Schweder; M. Hecker
• Keywords: Protein Synthesis Inhibitors; 0301 basic medicine; Binding Sites; Base Sequence; Molecular Sequence Data; RNA, Bacterial; 03 medical and health sciences; Chloramphenicol; Bacterial Proteins; RNA; Puromycin; RNA, Messenger; Rifampin; Ribosomes; Heat-Shock Proteins; Bacillus subtilis

In Bacillus subtilis IS58 starved of glucose or exposed to heat shock, ethanol or salt stress, the sigmaB-dependent general stress protein GsiB is accumulated to a higher level than other general stress proteins. This high-level accumulation of GsiB can at least partially be attributed to the remarkably long half-life (approximately 20 min) of the gsiB mRNA. Analysis of different gsiB-lacZ fusions revealed that this stability is not determined by sequences at the 3' end of the transcript but rather by sequences upstream of the translational start codon. Site-directed mutagenesis established that a strong ribosome binding site was crucial for the increased stability of the gsiB mRNA. A comparison of the sequences upstream of the translational start codons of three general stress genes, gsiB, gspA and ctc, revealed a direct correlation between mRNA stability and the strength of their translational signals.