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Gene Review:

regA - regulates translation of mRNAs for DNA...

Enterobacteria phage T4

Webster, K.R. et al., Adari, H.Y. et al., Winter, R.B. et al., Trojanowska, M. et al., Higgins, N.P. et al., et al.

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Disease relevance of regA

Bacteriophage T4 regA protein binds to mRNAs and prevents translation initiation [1].
Infection of Escherichia coli by a bacteriophage T4 regA, gene 44 double mutant leads to about a 7-fold increase in the amount of RNA ligase obtained after infection by wild-type phage [2].

High impact information on regA

A comparison of nucleotide sequences from several regA-repressed mRNAs suggests that the initiating AUG is an important, but not sufficient, sequence for regA binding [1].
We show here that purified regA protein binds specifically to target mRNAs near the initiating AUG and occludes binding of ribosomes [1].
Subsequently, an intact regA gene was cloned into plasmid pAS1 and overexpressed [3].
A DNA fragment carrying 85% of the coding sequence of regA has been cloned into the phage lambda leftward promoter PL expression vector pAS1, and a high level of truncated regA protein was produced by nalidixic acid induction [3].
The target for regA-mediated action overlaps the translational initiation domain of the rIIB messenger [4].

Biological context of regA

Translation of the DNA sequence predicted that regA protein contains 122 amino acids, with a Mr of 14,620 [3].
The structural gene for this polypeptide maps within a cluster of phage DNA replication genes, (genes 45-44-62-regA-43-42), all but one of which (gene 43) are under regA-mediated translational control [5].
The association constant (Ka) for regA protein binding to gene 44 RNA fragments was 100-fold higher than for binding to nontarget RNA [6].
The binding site size calculated for regA protein binding to poly(rU) was n = 9 +/- 1 nucleotides [6].
Mutagenesis of the COOH-terminal region of bacteriophage T4 regA protein [7].

Anatomical context of regA

Rather, the results suggest that the regA gene product may act either by interfering with early mRNA polypeptide chain initiation or by promoting prereplicative polysome dissociation [8].

Associations of regA with chemical compounds

Phenylalanine 106 was identified as the site of cross-linking, thus placing this residue at the interface of the regA protein-p(dT)16 complex [9].
Binding to nucleic acids was monitored by the quenching of the intrinsic tryptophan fluorescence of regA protein. regA protein exhibited differential affinities for the polynucleotides examined, with the order of affinity being poly(rU) greater than poly(dT) greater than poly(dU) = poly(rG) greater than poly(rC) = poly(rA) [6].

Other interactions of regA

In addition, there are sequence similarities in the translation initiation regions of genes 44, 45, and rIIB, all of which are subject to regulation by regA protein [10].

Analytical, diagnostic and therapeutic context of regA

Gel filtration through Sephadex G-75 revealed that wild-type and R91L regA proteins (14.6 kDa) elute at a mass of 29 kDa, consistent with the mass of a dimer [11].
Analysis of mRNA binding by filtration and nuclease protection assays shows that AUG is necessary but not sufficient for specific binding of regA protein to its mRNA targets [12].
(1973) to be defective in regulation of T4 protein synthesis, was shown by complementation tests to define a new gene, regA, and by intergenic mapping to lie between genes 43 and 62 [13].
Sequence analysis of conserved regA and variable orf43.1 genes in T4-like bacteriophages [14].

References

Bacteriophage T4 regA protein binds to mRNAs and prevents translation initiation. Winter, R.B., Morrissey, L., Gauss, P., Gold, L., Hsu, T., Karam, J. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
Bacteriophage T4 RNA ligase: preparation of a physically homogeneous, nuclease-free enzyme from hyperproducing infected cells. Higgins, N.P., Geballe, A.P., Snopek, T.J., Sugino, A., Cozzarelli, N.R. Nucleic Acids Res. (1977) [Pubmed]
Cloning, nucleotide sequence, and overexpression of the bacteriophage T4 regA gene. Adari, H.Y., Rose, K., Williams, K.R., Konigsberg, W.H., Lin, T.C., Spicer, E.K. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
Translational regulation: identification of the site on bacteriophage T4 rIIB mRNA recognized by the regA gene function. Karam, J., Gold, L., Singer, B.S., Dawson, M. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
The bacteriophage T4 regA gene: primary sequence of a translational repressor. Trojanowska, M., Miller, E.S., Karam, J., Stormo, G., Gold, L. Nucleic Acids Res. (1984) [Pubmed]
Characterization of bacteriophage T4 regA protein-nucleic acid interactions. Webster, K.R., Spicer, E.K. J. Biol. Chem. (1990) [Pubmed]
Mutagenesis of the COOH-terminal region of bacteriophage T4 regA protein. O'Malley, S.M., Sattar, A.K., Williams, K.R., Spicer, E.K. J. Biol. Chem. (1995) [Pubmed]
Level of specific prereplicative mRNA's during bacteriophage T4 regA-, 43- and T4 43- infection of Escherichia coli B. Trimble, R.B., Maley, n.u.l.l. J. Virol. (1976) [Pubmed]
Identification of amino acid residues at the interface of a bacteriophage T4 regA protein-nucleic acid complex. Webster, K.R., Keill, S., Konigsberg, W., Williams, K.R., Spicer, E.K. J. Biol. Chem. (1992) [Pubmed]
Bacteriophage T4 gene 44 DNA polymerase accessory protein. Sequences of gene 44 and its protein product. Spicer, E.K., Nossal, N.G., Williams, K.R. J. Biol. Chem. (1984) [Pubmed]
Bacteriophage T4 regA protein binds RNA as a monomer, overcoming dimer interactions. Phillips, C.A., Gordon, J., Spicer, E.K. Nucleic Acids Res. (1996) [Pubmed]
Binding of the bacteriophage T4 regA protein to mRNA targets: an initiator AUG is required. Unnithan, S., Green, L., Morrissey, L., Binkley, J., Singer, B., Karam, J., Gold, L. Nucleic Acids Res. (1990) [Pubmed]
Genetic mapping of regA mutants of bacteriophage T4D. Wiberg, J.S., Mendelsohn, S.L., Warner, V., Aldrich, C., Cardillo, T.S. J. Virol. (1977) [Pubmed]
Sequence analysis of conserved regA and variable orf43.1 genes in T4-like bacteriophages. Miller, E.S., Jozwik, C.E. J. Bacteriol. (1990) [Pubmed]

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