PubMed HealthSearch

Biomedical subjects

V Paces

Publications and source records attributed to V Paces.

At least 37 records · Page 2Linked to original sources

Comparison of genomes of closely related phages phi 29, phi 15 and PZA using a rapid method of parallel physical mapping.

The DNAs of phages phi 29, phi 15 and PZA of Bacillus subtilis were analysed with restriction enzymes EcoRI, HpaI and HindIII. A method was used which permits parallel physical mapping of all three phages, from both ends of their linear genomes. The method is based on transfer of partially digested DNA to DBM paper and sequential hybridization with labelled terminal fragments. It follows from the comparison of the physical maps that phages phi 29, phi 15 and PZA are closely related and that they probably have arisen from a common ancestor by accumulation of point mutations.

Bacillus subtilis

Nucleotide sequence of the major early region of Bacillus subtilis phage PZA, a close relative of phi 29.

The 5200-bp nucleotide sequence of the major early region of bacteriophage PZA has been determined. Open reading frames (ORFs) and potential transcriptional and translational regulatory signals were found in this region. The sequence was compared with the known sequence of the homologous region of the closely related phage phi 29 (Yoshikawa and Ito, 1982). This comparison permitted a more accurate assignment of several ORFs and regulatory signals.

Amino Acid Sequence

Cloning and expression in Escherichia coli of the synthetic proenkephalin analogue gene.

Enkephalins are pentapeptides with opioid activity that have been found in brain and other neural tissues. They are released by proteolytic processing of the proenkephalin, which contains several enkephalin sequences each flanked by pairs of basic amino acid (aa) residues. We have constructed an artificial variant of the proenkephalin gene by concatenation of synthetic oligodeoxynucleotides (oligo) coding for Met-enkephalin preceded by two arginines. One of the resulting structures, containing eleven enkephalin sequences separated by pairs of arginine codons, was cloned in the expression vector pRE31. The biological activity of enkephalin was detected after the digestion of the isolated plasmid-coded protein with trypsin and carboxypeptidase B. The product of the synthetic gene may thus serve as a defined simplified substrate for the study of the not yet fully understood enzymatic mechanisms of proenkephalin processing.

Animals