Seminalplasmin, an Antimicrobial Protein from Bull Seminal Plasma, Inhibits Growth, and Synthesis of Nucleic Acids and Proteins in S. cerevisiae

• Published in: Journal of biochemistry (Tokyo) Vol. 97; no. 2; pp. 463 - 471
• Main Authors: SCHEIT, Karl Heinz, SHIVAJI, Sisinthy, BHARGAVA, Pushpa M.
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 01.02.1985
• Subjects: Analytical, structural and metabolic biochemistry; Anti-Bacterial Agents; Anti-Infective Agents - pharmacology; Biological and medical sciences; Cell Nucleus - metabolism; DNA, Fungal - biosynthesis; Escherichia coli - drug effects; Escherichia coli - metabolism; Fundamental and applied biological sciences. Psychology; Fungal Proteins - biosynthesis; Miscellaneous; Mitochondria - metabolism; Proteins; Proteins - classification; Proteins - pharmacology; Protoplasts - metabolism; RNA, Fungal - biosynthesis; Saccharomyces cerevisiae; Saccharomyces cerevisiae - drug effects; Saccharomyces cerevisiae - growth & development; Saccharomyces cerevisiae - metabolism; Seminal Vesicle Secretory Proteins; Transcription, Genetic; Yeast; Bovine; Transcription; Growth; DNA synthesis; Antimicrobial agent; Proteins; RNA synthesis; Protein synthesis; Inhibition; Seminal plasma; Mechanism of action; Saccharomyces cerevisiae
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a135080

Seminalplasmin, an antimicrobial protein present in bovine seminal plasma, is shown to inhibit the growth of, as well as nucleic acid and protein synthesis in, wild-type Saccharomyces cerevisiae SM202, when used at concentrations > 200 μg/ml, in contrast to 20 ug/ml that is sufficient for Escherichia coli. An osmotically labile strain of S. cerevisiae VY1160 is 1–2 orders of magnitude more sensitive to seminalplasmin than the wild-type strain. RNA synthesis in protoplasts and nuclei of S. cerevisiae SM 202 was also about as sensitive to seminalplasmin as in E. coli and S. cerevisiae VY1160. The RNA polymerases I and II from S. cerevisiae were strongly inhibited by seminalplasmin in vitro, while DNA and protein syntheses were not affected by seminalplasmin in cell-free systems, unlike in the whole cells. It is concluded that seminalplasmin acts in S. cerevisiae by entering the cells and inhibiting transcription.