Trumbore M W, Berger S L
Section on Genes and Gene Products, National Cancer Institute, National Institutes of Health, Building 8, Room 311A, Bethesda, Maryland 20892-0480, USA.
Protein Expr Purif. 2000 Dec;20(3):414-20. doi: 10.1006/prep.2000.1332.
The effect of prothymosin alpha on transcriptional elongation has been examined. The addition of prothymosin alpha to COS-1 and NIH3T3 cell nuclei engaged in run-on transcription stimulated RNA synthesis approximately two- to threefold in a dose-dependent manner. Polyglutamic acid or a random polypeptide composed of glutamic acid, alanine, and tyrosine, did not substitute for prothymosin alpha. Enhanced transcription occurred in the presence of high and low doses of actinomycin D and in the presence of alpha-amanitin, but not in nuclear extracts. The stimulatory effect was dependent on a limiting concentration of one nucleoside triphosphate and was nearly abrogated by saturating levels of precursors. In the presence of Sarkosyl, which itself increases transcription, prothymosin alpha was almost ineffectual. The data are consistent with a model in which prothymosin alpha does not interact directly with polymerases but, instead, nonspecifically decreases the barriers to diffusion of charged molecules in electrostatically charged environments.
