Biochemical characterization and posttranslational modification of AlgU, a regulator of stress response in Pseudomonas aeruginosa


Por: Schurr M.J., Yu H., Martinez-Salazar J.M., Hibler N.S., Deretic V.

Publicada: 1 ene 1995
Resumen:
AlgU is homologous to the extreme heat shock sigma factor ?(E) from enteric bacteria. In this work, AlgU was overproduced and purified and its function investigated at the biochemical level. AlgU was shown to associate with RNA polymerase and direct transcription of a target promoter. AlgU also exhibited multiple isoforms detected by 2D gel analysis. Treatment with a Ser/Thr phosphatase shifted the distribution of isoforms towards the basic side on 2D gels, suggesting that posttranslational modifications of AlgU may involve phosphorylation. The underphosphorylated forms of AlgU copurified with RNA polymerase. It is possible that phosphorylation affects AlgU activity or its stability.

Filiaciones:
Schurr M.J.:
 Department of Microbiology, University of Texas, Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7758, United States

Yu H.:
 Department of Microbiology, University of Texas, Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7758, United States

Martinez-Salazar J.M.:
 Department of Microbiology, University of Texas, Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7758, United States

Hibler N.S.:
 Department of Microbiology, University of Texas, Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7758, United States

Deretic V.:
 Department of Microbiology, University of Texas, Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7758, United States
ISSN: 0006291X
Editorial
ACADEMIC PRESS INC ELSEVIER SCIENCE, 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA, Estados Unidos America
Tipo de documento: Article
Volumen: 216 Número: 3
Páginas: 874-880
WOS Id: A1995TF71300020
ID de PubMed: 7488207

MÉTRICAS