HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Spudich, J. L. Articles by Stoeckenius, W. Search for Related Content PubMed PubMed Citation Articles by Spudich, J. L. Articles by Stoeckenius, W. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 255, Issue 12, 5501-5503, Jun, 1980

Light-regulated retinal-dependent reversible phosphorylation of Halobacterium proteins

JL Spudich and W Stoeckenius

By (32P)orthophosphate pulse-labeling in vivo, we have identified a class of phosphoproteins in Halobacterium halobium. Exposing labeled whole cells to light results in a rapid dephosphorylation of two of the proteins, which are rapidly rephosphorylated upon darkening of the cells. The light sensitivity of these two proteins is abolished by the retinal synthesis inhibitor nicotine and is restored upon addition of exogenous retinal to the cells. This indicates that the dephosphorylation depends on the rhodopsin-like (retinal-containing) photoreceptors of this organism. Retinal pigments, one of which is the retinyldene protein bacteriorhodopsin, are responsible for both photoenergy and photosensory transduction by Halobacterium. The light- regulated phosphoproteins are of molecular weights of approximately 80,000 and 100,000. Acid and hydroxylamine resistance of the phosphate bonds in both proteins suggests phosphoserine or phosphothreonine linkages.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Eichler and M. W. W. Adams Posttranslational Protein Modification in Archaea Microbiol. Mol. Biol. Rev., September 1, 2005; 69(3): 393 - 425. [Abstract] [Full Text] [PDF]

				B. H. Lower, M. B. Potters, and P. J. Kennelly A Phosphoprotein from the Archaeon Sulfolobus solfataricus with Protein-Serine/Threonine Kinase Activity J. Bacteriol., January 15, 2004; 186(2): 463 - 472. [Abstract] [Full Text] [PDF]

				B. H. Lower and P. J. Kennelly Open Reading Frame sso2387 from the Archaeon Sulfolobus solfataricus Encodes a Polypeptide with Protein-Serine Kinase Activity J. Bacteriol., June 1, 2003; 185(11): 3436 - 3445. [Abstract] [Full Text] [PDF]

				B. H. Lower and P. J. Kennelly The Membrane-Associated Protein-Serine/Threonine Kinase from Sulfolobus solfataricus Is a Glycoprotein J. Bacteriol., May 15, 2002; 184(10): 2614 - 2619. [Abstract] [Full Text] [PDF]

				B. H. Lower, K. M. Bischoff, and P. J. Kennelly The Archaeon Sulfolobus solfataricus Contains a Membrane-Associated Protein Kinase Activity That Preferentially Phosphorylates Threonine Residues In Vitro J. Bacteriol., June 15, 2000; 182(12): 3452 - 3459. [Abstract] [Full Text]