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J W Roberts

Publications and source records attributed to J W Roberts.

122 records · Page 7Linked to original sources

Escherichia coli recA gene product inactivates phage lambda repressor.

Phage lambda repressor is inactivated and cleaved into two detectable fragments during incubation with purified Escherichia coli recA gene protein in vitro, in a reaction that requires ATP. This reaction reproduces the recA-dependent inactivation of repressor that occurs in vivo during induction of the SOS functions. The proteolytic activity may reside in the recA protein itself and may be a fundamental activity of it.

Adenosine Triphosphate↗

Inactivation and proteolytic cleavage of phage lambda repressor in vitro in an ATP-dependent reaction.

We have reproduced in vitro the inactivation of bacteriophage lambda repressor that occurs in vivo when a lambda lysogen is treated with agents such as ultraviolet radiation that attack DNA. ATP and a divalent cation are required for the inactivation reaction. The ind- repressor is insensitive to the inactivation mechanism. A proteolytic cleavage of repressor accompanies inactivation in vitro, as it does in vivo.

Adenosine Triphosphate↗

Nucleotide sequence studies of normal and genetically altered glycine transfer ribonucleic acids from Escherichia coli.

The total nucleotide sequence of tRNAGGA/G -Gly2 from Escherichia coli is pG-C-G-G-G-C-A-U-C-G-U-A-U-A-A-U-G-G-C-U-A-U-U-A-C-C-U-C-A-G-C-C-U-N-C-C-A-A-G-C-U-G-A-U-G-A-U-G-C-G-G-G-T-psi-C-G-A-U-U-C-C-C-G-C-U-G-C-C-C-G-C-U-C-C-AOH, where T- at position 53 is ribothymidylic acid, and psi- at position 54 is pseudouridylic acid; N- at position 36 is an unidentified derivative of uridylic acid, and is present in modified form in a portion of tRNAGGA/G -Gly 2 molecules isolated from E. coli cells. The missense suppressor mutation, glyTsuA36(HA), results in a C yields U base substitution at the 3' end of the anticodon of tRNAGGA/G -Gly 2 (nucleotide position 38). A secondary effect of this base substitution is the modification of the A residue directly adjacent to the 3' end of the anticodon of tRNAsuA36(HA), -Gly 2 suggesting that the enzymes responsible for this modification recognize the anticodon sequences of prospective tRNA substrates. The creation of a missense-suppressing tRNA, tRNAsuA36(HA), -Gly 2 by an alteration of the anticodon sequence of tRNAGGA/G -Gly 2 is analogous to mechanisms whereby other suppressor tRNAs have arisen. The high degree of nucleotide sequence homology between the amino acid acceptor stems and anticodon regions of four glycine isoaccepting tRNAs specified by E. coli and bacteriophage T4 suggests that these regions may be recognized by the glycyl-tRNA synthetase; the involvement of the anticodon region in the synthetase recognition process is supported by the greatly decreased rate of aminoacylation of tRNAsuA36(HA) -Gly 2.

Anticodon↗

Proteolytic cleavage of bacteriophage lambda repressor in induction.

The bacteriophage lambda repressor, a protein that maintains the lysogenic state of a bacterium containing a lambda prophage, is cleaved when the lysogen is induced by mitomycin C or ultraviolet light. This cleavage does not occur when induction is prevented by mutational alteration either of the phage repressor or of the host recA gene product. Proteolytic cleavage may be the primary mechanism of repressor inactivation in this induction pathway, or it may follow a different event which causes the initial inactivation.

Coliphages↗

Transcription termination and late control in phage lambda.

A transcription termination site occurs between the promoter for late gene expression of bacteriophage lambda and the late genes themselves. It is proposed that the lambda Q gene product controls late gene expression by over-coming this termination barrier.

Cell-Free System↗

A brief consideration of the SOS inducing signal.

SOS functions are induced in E. coli by treatments that damage cellular DNA or interrupt its synthesis. The biochemical basis of induction is activation of the specific proteolytic activity of recA protein, which then inactivates the lexA repressor. We discuss the development of the inducing signal in the cell.

Bacterial Proteins↗