An unusual mechanism of bacterial gene expression revealed for the RNase P protein of Thermus strains.
The RNase P protein gene (rnpA) completely overlaps the rpmH gene (encoding ribosomal protein L34) out of frame in the thermophilic bacterium Thermus thermophilus. This results in the synthesis of an extended RNase P protein (C5) of 163 aa and, by inference, of 240 aa in the related strain Thermus filiformis. Start codons of rnpA and rpmH, apparently governed by the same ribosome binding site, are separated by only 4 nt, which suggests a regulatory linkage between L34 and C5 translation and, accordingly, between ribosome and RNase P biosynthesis. Within the sequence encoding the N-terminal extensions and downstream of rpmH, several Thermus species exhibit in-frame deletionsinsertions, suggesting relaxed constraints for sequence conservation in this region. Roughly the N-terminal third of T. thermophilus C5 was further shown to be dispensable for RNase P function in vitro by using a precursor tRNA(Gly) substrate from the same organism. Taken together, these data reveal a mode of gene expression that is to our knowledge unprecedented in bacteria.
Institute für Biochemie and Molekulare Medizin, Universität zu Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany.
Ralph
R
Feltens
Markus
M
Gossringer
Dagmar K
DK
Willkomm
Henning
H
Urlaub
Roland K
RK
Hartmann
D000595:Amino Acid Sequence; D001483:Base Sequence; D004722:Endoribonucleases / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D008969:Molecular Sequence Data; D016337:RNA, Catalytic / Q000235:genetics* / Q000378:metabolism; D043262:Ribonuclease P; D012261:Ribonucleoproteins / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics*
D016337:RNA, Catalytic; D012261:Ribonucleoproteins; D004722:Endoribonucleases; D043262:Ribonuclease P