DOI: 10.1128/jb.117.3.1231-1239.1974. Inhibition of <i>lacZ</i> Gene Translation Initiation in <i>trp-lac</i> Fusion Strains

Inhibition of lacZ Gene Translation Initiation in trp-lac Fusion Strains

10.1128/jb.117.3.1231-1239.1974

Crossref journal-article

American Society for Microbiology

Journal of Bacteriology (235)

Abstract

Different levels of β-galactosidase are found in various trp-lac fusion strains. These levels of β-galactosidase fall within a 60-fold range. The amount of thiogalactoside transacetylase activity detected in these same strains only varies 10-fold and is found in amounts greater than those predicted from the β-galactosidase levels. The observation that the β-galactosidase and thiogalactoside transacetylase levels are not directly proportional, that the lacZ messenger ribonucleic acid (mRNA) levels are not proportional to the β-galactosidase activity, that, at least for the one fusion strain tested, the SuA polarity suppressor does not affect the β-galactosidase level, and that, in all but one strain, the β-galactosidase activity appears to reside in normal β-galactosidase molecules suggests that the disproportionately low production of β-galactosidase is due to a decrease in the frequency of translation initiation of lacZ mRNA in these strains. Several mechanisms are proposed to explain this decrease. Some possible bases for the disproportional production of β-galactosidase and thiogalactoside transacetylase are also described. The preferred explanation for these disproportional enzyme levels is that only a fraction of the full complement of ribosomes need initiate translation at lacZ for the functional synthesis of lac mRNA to occur and that once the lac ribonucleic acid is made a full complement of ribosomes can bind at internal translation initiation sites at Y and A .

Bibliography

Reznikoff, W. S., Michels, C. A., Cooper, T. G., Silverstone, A. E., & Magasanik, B. (1974). Inhibition of lacZ Gene Translation Initiation in trp-lac Fusion Strains. Journal of Bacteriology, 117(3), 1231â1239.

Authors 5

William S. Reznikoff (first)
Corinne A. Michels (additional)
Terrance G. Cooper (additional)
Allen E. Silverstone (additional)
Boris Magasanik (additional)

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Dates

Type	When
Created	5 years, 7 months ago (Jan. 3, 2020, 9:57 a.m.)
Deposited	4 years ago (July 29, 2021, 1:12 p.m.)
Indexed	1 year, 7 months ago (Jan. 15, 2024, 12:18 p.m.)
Issued	51 years, 5 months ago (March 1, 1974)
Published	51 years, 5 months ago (March 1, 1974)
Published Print	51 years, 5 months ago (March 1, 1974)

Funders 0

None

BibTeX

@article{Reznikoff_1974, title={Inhibition of lacZ Gene Translation Initiation in trp-lac Fusion Strains}, volume={117}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.117.3.1231-1239.1974}, DOI={10.1128/jb.117.3.1231-1239.1974}, number={3}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Reznikoff, William S. and Michels, Corinne A. and Cooper, Terrance G. and Silverstone, Allen E. and Magasanik, Boris}, year={1974}, month=mar, pages={1231–1239} }

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  "abstract": "<jats:p>\n            Different levels of \u03b2-galactosidase are found in various\n            <jats:italic>trp-lac</jats:italic>\n            fusion strains. These levels of \u03b2-galactosidase fall within a 60-fold range. The amount of thiogalactoside transacetylase activity detected in these same strains only varies 10-fold and is found in amounts greater than those predicted from the \u03b2-galactosidase levels. The observation that the \u03b2-galactosidase and thiogalactoside transacetylase levels are not directly proportional, that the\n            <jats:italic>lacZ</jats:italic>\n            messenger ribonucleic acid (mRNA) levels are not proportional to the \u03b2-galactosidase activity, that, at least for the one fusion strain tested, the SuA polarity suppressor does not affect the \u03b2-galactosidase level, and that, in all but one strain, the \u03b2-galactosidase activity appears to reside in normal \u03b2-galactosidase molecules suggests that the disproportionately low production of \u03b2-galactosidase is due to a decrease in the frequency of translation initiation of\n            <jats:italic>lacZ</jats:italic>\n            mRNA in these strains. Several mechanisms are proposed to explain this decrease. Some possible bases for the disproportional production of \u03b2-galactosidase and thiogalactoside transacetylase are also described. The preferred explanation for these disproportional enzyme levels is that only a fraction of the full complement of ribosomes need initiate translation at\n            <jats:italic>lacZ</jats:italic>\n            for the functional synthesis of\n            <jats:italic>lac</jats:italic>\n            mRNA to occur and that once the\n            <jats:italic>lac</jats:italic>\n            ribonucleic acid is made a full complement of ribosomes can bind at internal translation initiation sites at\n            <jats:italic>Y</jats:italic>\n            and\n            <jats:italic>A</jats:italic>\n            .\n          </jats:p>",
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