Search PubMed⌕ Search

Biomedical subjects

T A Bickle

Publications and source records attributed to T A Bickle.

At least 91 records · Page 5Linked to original sources
PubMed1982

The catabolite-sensitive promoter for the chloramphenicol acetyl transferase gene is preceded by two binding sites for the catabolite gene activator protein.

DNase I protection experiments have indicated that the cyclic AMP-catabolite gene activator protein complex binds to two regions preceding the chloramphenicol acetyl transferase (cat) gene in Escherichia coli. One of these lies adjacent to the RNA polymerase binding site, whereas the second lies approximately 130 base pairs upstream from the starting point of transcription. Additional DNase protection experiments and in vitro transcription experiments with modified templates indicate that the catabolite gene activator protein site proximal to the cat promoter functions independently of the distal site, indicating that in vitro the second of these sites is not required for transcriptional activation of the cat gene.

Acetyltransferases↗
PubMed1981

The DNA sequence of the phage lambda genome between PL and the gene bet.

We have determined 3,400 base pairs of DNA sequence from the phage gamma genome which starts to the right of PL and runs to the left into the gene bet. The sequence thus includes the genes, N, ral, Ea10, cIII, kil and gam, as well as the transcription terminators TL1 and TL2. One surprising feature of the sequence is the presence in the region expected to be occupied by ral of a long open reading frame that, if it is expressed, would have to be transcribed from left to right, or counter to transcription from PL.

Bacteriophage lambda↗
PubMed1981

Purification and properties of the restriction endonuclease BglII from Bacillus globigii.

The restriction endonuclease BglII from Bacillus globigii has been purified to homogeneity. The enzyme is a dimer of two subunits of Mr = 27000. The reaction mechanism does not involve the accumulation of a DNA intermediate nicked in one strand and the enzyme is not affected by superhelical twists in the substrate DNA, indicating that DNA binding does not involve either winding or unwinding of the double helix. Antibodies were prepared against BglII. These antibodies did not cross react with any other restriction endonucleases tested, including other enzymes from B. globigii or from closely related strains. It is thus unlikely that type II restriction enzymes represent a closely related group of proteins.

Animals↗
PubMed1980

The DNA sequence recognised by BglI.

The restriction enzyme BglI recognizes the DNA sequence: (Formula: see text) and cleaves it in the position shown by the arrows to leave 3' single-stranded protrusions three bases long.

Bacillus↗
PubMed1979

A novel bacteriophage defence mechanism: the anti-restriction protein.

Bacteriophage T3 and T7 protect their DNA from restriction by producing, as the earliest detectable phage functions, anti-restriction proteins. Although the two phage proteins differ in their chromatographic and antigenic properties, they act by the same mechanism: the anti-restriction proteins inhibit E. coli K12 restriction endonuclease by direct interaction.

Coliphages↗
PubMed1977

A simple, general procedure for purifying restriction endonucleases.

A simple, general method for purifying restriction endonucleases is described. The method employs precipitation of nucleic acids from crude extracts with polyethyleneimine followed by affinity chromatography on columns of heparin covalently linked to agarose. Most of the sixteen enzymes tested could be purified to a degree sufficient for DNA sequencing work by this method sometimes supplemented by at most one step of ion exchange chromatography.

Bacillus↗