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At least 685 records · Page 38Linked to original sources
PubMed1991

The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces.

The actII region, flanked by biosynthetic genes in the 25 kb act cluster of S. coelicolor, consists of four open reading frames, including a transcriptional activator for the biosynthetic genes, and genes controlling antibiotic export. A TTA codon (extremely rare in Streptomyces) is present both in actII-ORF2 (encoding a putative transmembrane export protein) and actII-ORF4 (the transcriptional activator gene). Change of the TTA in ORF4 to TTG reverses the normal interruption of actinorhodin synthesis caused by mutation in the pleiotropic regulatory gene bldA (which encodes the cell's tRNA(Leu)(UUA)). We conclude that initiation of actinorhodin synthesis via the actII-ORF4 product, and the final step in production, antibiotic export, are twin targets via which bldA exerts developmental control of actinorhodin production.

Amino Acid Sequence↗
PubMed1990

Search of the 5' untranslated region of the human cardiac actin gene for segments controlling translation.

We have examined the possibility that the 5'-UT region of the human cardiac actin (CH-actin) mRNA is responsible for regulating translation of this transcript during skeletal myogenesis. Genes were constructed which consisted of the murine leukaemia virus promoter driving the Escherichia coli LacZ coding region with and without the CH-actin 5'-UT region. These constructs were transfected into L6 myoblasts that were subsequently differentiated into myotubes. The presence of the CH-actin 5'-UT region appeared to have no effect on expression of the LacZ reporter gene. EGTA blocks myogenesis and inhibits translation of muscle-specific transcripts (Endo, T. and Nadal-Ginard, B. (1987) Cell 49, 515-526) but EGTA had no effect on expression of the chimaeric LacZ transcripts. Thus, if the CH-actin transcript is subject to translational regulation, it must be mediated by sequences other than those of the 5'-UT region.

Actins↗
PubMed1988

Translational control by antisense RNA in control of plasmid replication.

Control of replication of plasmids involves two processes: measurement of the copy number of the plasmid and adjustment of the replication frequency accordingly. For both these processes IncFII plasmids use an antisense RNA (CopA RNA) that forms a duplex with the upstream region (CopT) of the mRNA of the rate-limiting RepA protein. The kinetics of duplex formation was measured in vitro for the wild type and for a cop mutant plasmid; the mutant showed a reduction in the second-order rate constant for the formation of the RNA duplex and a similar increase in copy number. Hence, the kinetics of duplex formation and the concentration of CopA RNA determines the copy number of the plasmid.

Base Sequence↗
PubMed2002

NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.

L20 is a specific protein of the bacterial ribosome, which is involved in the early assembly steps of the 50S subunit and in the feedback control of the expression of its own gene. This dual function involves specific interactions with either the 23S rRNA or its messenger RNA. The solution structure of the free Aquifex aeolicus L20 has been solved. It is composed of an unstructured N-terminal domain comprising residues 1-58 and a C-terminal alpha-helical domain. This is in contrast with what is observed in the bacterial 50S subunit, where the N-terminal region folds as an elongated alpha-helical region. The solution structure of the C-terminal domain shows that several solvent-accessible, conserved residues are clustered on the surface of the molecule and are probably involved in RNA recognition. In vivo studies show that this domain is sufficient to repress the expression of the cistrons encoding L35 and L20 in the IF3 operon. The ability of L20 C-terminal domain to specifically recognise RNA suggests an assembly mechanism for L20 into the ribosome. The pre-folded C-terminal domain would make a primary interaction with a specific site on the 23S rRNA. The N-terminal domain would then fold within the ribosome, participating in its correct 3D assembly.

Amino Acid Sequence↗