Biomedical subjects

Andrew Hesketh

Publications and source records attributed to Andrew Hesketh.

3 recordsLinked to original sources

PubMed2004

PEDRo: a database for storing, searching and disseminating experimental proteomics data.

BACKGROUND: Proteomics is rapidly evolving into a high-throughput technology, in which substantial and systematic studies are conducted on samples from a wide range of physiological, developmental, or pathological conditions. Reference maps from 2D gels are widely circulated. However, there is, as yet, no formally accepted standard representation to support the sharing of proteomics data, and little systematic dissemination of comprehensive proteomic data sets. RESULTS: This paper describes the design, implementation and use of a Proteome Experimental Data Repository (PEDRo), which makes comprehensive proteomics data sets available for browsing, searching and downloading. It is also serves to extend the debate on the level of detail at which proteomics data should be captured, the sorts of facilities that should be provided by proteome data management systems, and the techniques by which such facilities can be made available. CONCLUSIONS: The PEDRo database provides access to a collection of comprehensive descriptions of experimental data sets in proteomics. Not only are these data sets interesting in and of themselves, they also provide a useful early validation of the PEDRo data model, which has served as a starting point for the ongoing standardisation activity through the Proteome Standards Initiative of the Human Proteome Organisation.

Animals↗

PubMed2003

Evidence from proteomics that some of the enzymes of actinorhodin biosynthesis have more than one form and may occupy distinctive cellular locations.

An important attribute of proteome analysis carried out with the aid of two-dimensional gel electrophoresis is that post-translational modifications of proteins can often be revealed. Large-scale proteomic analysis of Streptomyces coelicolor A3(2) has been made possible with the availability of its genome sequence. Here, we bring together observations on the proteins specifically associated with biosynthesis of the isochromanequinone polyketide antibiotic actinorhodin. The predicted products of 14 of the genes annotated as belonging to the act gene cluster were detected. They were generally present only in stationary phase cultures. Plausible explanations are presented for the absence of the other nine. For six of the gene products detected, there was evidence of either specific processing or covalent modification; in the case of the pyran ring closure enzyme ActVI-ORF3, the cleavage of the N-terminal 31 or 34 amino acids was previously shown to be associated with an extracytoplasmic location for the mature gene product. These observations may have implications for the regulation of actinorhodin biosynthesis, and for biochemical studies of artificially expressed Act proteins.

3-Hydroxyacyl CoA Dehydrogenases↗

PubMed1997

Expression analysis of the ssgA gene product, associated with sporulation and cell division in Streptomyces griseus.

The ssgA gene of Streptomyces griseus B2682, when present in high copy number, results in both suppression of sporulation and fragmented growth of mycelia. Western analysis with polyclonal antibodies against the gene product (SsgA) revealed a close correlation between SsgA accumulation and the onset of sporulation in wild-type cells. The protein was only detected in the cytoplasm. Certain developmental mutants of S. griseus (afs, reIC and brgA) which are defective in aerial mycelium formation in solid culture and submerged spore formation in liquid culture failed to accumulate SsgA. The SsgA protein appeared shortly (1 h) after nutritional shift-down of strain B2682 cells. afs mutant cells sporulated and expressed SsgA only when A-factor was present both before and after nutritional shift-down. Introduction of the ssgA gene in a low-copy-number vector into strain B2682 resulted in fivefold overexpression of SsgA, and was accompanied by fragmented growth of mycelia and suppression of submerged spore formation (in liquid culture) and aerial mycelium formation (in solid culture). Streptomycin production was not inhibited. In a control experiment, a nonfunctional ssgA gene possessing a frameshift mutation near its N-terminus had no effect on either growth or sporulation. It is proposed that the ssgA gene product plays a role in promoting the developmental process of S. griseus.

Amino Acid Sequence↗