lacZ translation initiation mutations

Munson, Lianna M.; Stormo, Gary D.; Niece, Ronald L.; Reznikoff, William S.

doi:10.1016/0022-2836(84)90043-3

Cited by 109 publications

(61 citation statements)

References 27 publications

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“…Examples of such features are given in reference 62. Similar results have been obtained with point mutations in the start triplet of the lacZ gene (89,132).…”

Section: Translational Initiationsupporting

confidence: 84%

Evolutionary Conservation of Reactions in Translation

Ganoza

Kiel

Aoki

2002

Microbiol Mol Biol Rev

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SUMMARY Current X-ray diffraction and cryoelectron microscopic data of ribosomes of eubacteria have shed considerable light on the molecular mechanisms of translation. Structural studies of the protein factors that activate ribosomes also point to many common features in the primary sequence and tertiary structure of these proteins. The reconstitution of the complex apparatus of translation has also revealed new information important to the mechanisms. Surprisingly, the latter approach has uncovered a number of proteins whose sequence and/or structure and function are conserved in all cells, indicating that the mechanisms are indeed conserved. The possible mechanisms of a new initiation factor and two elongation factors are discussed in this context.

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“…Examples of such features are given in reference 62. Similar results have been obtained with point mutations in the start triplet of the lacZ gene (89,132).…”

Section: Translational Initiationsupporting

confidence: 84%

Evolutionary Conservation of Reactions in Translation

Ganoza

Kiel

Aoki

2002

Microbiol Mol Biol Rev

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“…It is of particular interest to note that, in each case (CAA, TCA, TTC) where the new second codon introduced a four-base sequence complementary to the 5'-terminal sequence of 16S RNA immediately after the first ATG initiation codon, the expression of the gene was drastically reduced (Looman et al, 1987). Interpretation of these results in the light of our hypothesis is complicated by the fact that secondary 3960 structure involving both initiation codons is believed to play an important role in the regulation of the translational initiation of this gene (Munson et al, 1984) and that the effect of these mutations on this secondary structure may be more important than the introduction of a new downstream interaction of the type that we propose. Equally, however, these results might be taken to indicate that a strong downstream interaction with the 16S RNA that is close to the ATG initiation codon has the effect of reducing translational efficiency.…”

Section: Statistical Considerationsmentioning

confidence: 76%

“…Of the 251 entries in our file, 168 (66.9% of the total file) contain a sequence of at least four consecutive nucleotides and 47 of those 168 (18.7% of the total file) have a sequence of five or more consecutive nucleotides that is complementary to the 5'-terminal sequence of E.coli 16S RNA. The calculations of probability of occurrence assume that the four nucleotides are randomly distributed in E. coli gene starts and ignores the fact that, for example, the sequences immediately following the initiation codon tend to be low in G residues (Stormo et al, 1982a (Munson et al, 1984). This gene obeys our rule, since the tetramer TTCA is found within the proposed range of both of the two initiation codons.…”

Section: Statistical Considerationsmentioning

confidence: 99%

Messenger RNA recognition in Escherichia coli: a possible second site of interaction with 16S ribosomal RNA.

1988

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Examination of the nucleotides following the ATG or GTG initiation codons of a file of 251 genes from Escherichia coli has shown that 247 (98.4%) of them contain a sequence of at least three and 168 (66.9%) of them a sequence of at least four consecutive nucleotides that is complementary to some part of the 16 nt at the 5' terminus of the bacterial 16S rRNA. It is proposed that this sequence, which falls within the first 24 nt coding for the genetic message, might be involved in mRNA recognition through a mechanism analogous to the wellestablished 'Shine-Dalgarno' interaction with the 3' terminus of the 16S rRNA. Comparison of these data with data derived from a file of 117 'false' gene starts that have a Shine-Dalgarno-like sequence followed by a suitably spaced ATG or GTG triplet but which are believed not to lie at the beginnings of genetic messages shows the association that we have found to be statistically significant at the 99.9% level.

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“…7 , lanes 2 and 3). One explanation for this might be that the deletions changed the conformation of the ribosome binding regions in the transcript, thus decreasing the translation of the following cistron [45,46]. The fact that the construction pKTHl501 A6 decreased the signal of the 28-kDa b protein, but not that of the 18-kDa protein and that the construction pKTHl Sold5 decreased only the signal of the IS-kDa protein but not that of the 28-kDa protein a suggests that the halflives of the deleted transcripts were not affected.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of a 2.2‐kb operon preceding the α‐amylase gene of Bacillus amyloliquefaciens

Kallio

Ulmanen

Palva

1986

European Journal of Biochemistry

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A DNA region of 2.8 x lo3 base pairs (2.8 kb) upstream of the Bacillus amyloliquefaciens a-amylase gene has been isolated. This DNA gave rise to a 2.2-kb transcript. The 3' end of the transcript was mapped with S1 nuclease and shown to terminate 49 base pairs upstream of the -35 region of the a-amylase promoter. In B. subtilis minicells this 2.2-kb transcript coded for three different polypeptides, thus indicating a polycistronic operon-type structure. The location and the order of the polypeptides were established using DNA deletions. The joining of the 2.2-kb operon to the downstream a-amylase gene in the plasmid PUB110 did not have any significant effect on the level of expression of the a-amylase.Bacilli are known to produce a wide variety of exoenzymes some of which, like a-amylases and proteases, are of commercial importance. At present the a-amylases are the best characterized group of exoenzymes and a-amylase genes have been cloned from various Bacillus species [l -101.In our laboratory the a-amylase gene from B. amyloliquefaciens has been cloned in B. subrilis using the plasmid pUBllO as the vector [3]. The gene has been completely sequenced [ 1 I] and the transcription initiation and termination sites determined [12]. In addition, a set of expression/ secretion vectors have been constructed from the promotersignal sequence region of the a-amylase gene and used to study the expression of foreign genes in B. subtilis [13-151. However, very little is known about the regulation of the expression of the a-amylase genes. Only the a-amylase gene from B. subtilis has been studied at the genetic level. The available data suggest that several loci specifically affect the level of a-amylase production. Some of these loci are closely linked to the structural gene of a-amylase (amyR2, amyR3, tmrA) while others have been mapped elsewhere (amyS [16]). These loci are known to enhance the a-amylase production but the mechanism of this effect at the molecular level is unclear. We have previously tested whether the presence of any of the above loci would effect the expression of the B. amyloliquefaciens a-amylase clone in B. subtilis, but no positive response could be demonstrated [17].In this paper we report the isolation and characterization of a 2.8-kb DNA fragment upstream of the B. amyloliquefaciens a-amylase gene. This 2.8-kb DNA was shown to contain a 2.2-kb operon giving rise to three different polypeptides. However, this operon, when joined to the a-amylase clone, did not affect the production of B. amyloliquefaciens a-amylase in B. subtilis. MATERIALS AND METHODS Bacteria and plasmidsBacillus amyloliquefaciens strain El 8 [ 181 was used for the isolation of total chromosomal DNA to clone the DNA region upstream of the a-amylase gene.B. subtilis BRBl (previously named IH6064) and BRB152 (amy-) were from our collection [9]. A minicell producing B. subtilis strain CUM3 [divIVBl, metB5, thyAl, thyB1, spo(-)] was obtained from Bacillus Genetic Stock Center (Columbus, Ohio, USA; 1A197 in BGSC).Plasmids pKTH10, pKTH2O...

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lacZ translation initiation mutations

Cited by 109 publications

References 27 publications

Evolutionary Conservation of Reactions in Translation

Evolutionary Conservation of Reactions in Translation

Messenger RNA recognition in Escherichia coli: a possible second site of interaction with 16S ribosomal RNA.

Isolation and characterization of a 2.2‐kb operon preceding the α‐amylase gene of Bacillus amyloliquefaciens

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