The Photoactive Yellow Protein from Ectothiorhodospira Halophila As Studied with a Highly Specific Polyclonal Antiserum: (intra)cellular Localization, Regulation of Expression, and Taxonomic Distribution of Cross-reacting Proteins

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1994 Jul 1

PMID 8021174

Citations 6

Authors

W D Hoff

W W Sprenger

P W Postma

T E Meyer

M Veenhuis

T Leguijt

K J Hellingwerf

Affiliations

Soon will be listed here.

Abstract

A rabbit antiserum was raised against the photoactive yellow protein (PYP) from Ectothiorhodospira halophila and purified by adsorption experiments to obtain a highly specific polyclonal antiserum. This antiserum was used to obtain the following results. (i) In E. halophila, PYP can be isolated from the fraction of soluble proteins. In the intact cell, however, PYP appeared to be associated with (intra)cytoplasmic membranes, as was concluded from analysis of immunogold-labelled thin sections of the organism. (ii) The regulation of expression of PYP was studied by using dot blot assays, Western blotting (immunoblotting), and rocket immunoelectrophoresis. Under all conditions investigated (light color, salt concentration, and growth phase), PYP was expressed constitutively in E. halophila. However, when Rhodospirillum salexigens was grown aerobically, the expression of PYP was suppressed. (iii) A large number of prokaryotic microorganisms contained a single protein, with an apparent size of approximately 15 kDa, that cross-reacted with the antiserum. Among the positively reacting organisms were both phototrophic and chemotrophic, as well as motile and nonmotile, organisms. After separation of cellular proteins into a membrane fraction and soluble proteins, it was established that organisms adapted to growth at higher salt concentrations tended to have the cross-reacting protein in the soluble fraction. In the cases of R. salexigens and Chromatium salexigens, we have shown that the cross-reacting protein involved is strongly homologous to PYP from E. halophila.

Citing Articles

Protein folding thermodynamics applied to the photocycle of the photoactive yellow protein.

van Brederode M, Hoff W, van Stokkum I, Groot M, Hellingwerf K Biophys J. 1996; 71(1):365-80.

PMID: 8804619 PMC: 1233487. DOI: 10.1016/S0006-3495(96)79234-2.

The xanthopsins: a new family of eubacterial blue-light photoreceptors.

Kort R, Hoff W, Van West M, Kroon A, Hoffer S, Vlieg K EMBO J. 1996; 15(13):3209-18.

PMID: 8670821 PMC: 451869.

Photobiology of bacteria.

Hellingwerf K, Crielaard W, Hoff W, Matthijs H, Mur L, van Rotterdam B Antonie Van Leeuwenhoek. 1994; 65(4):331-47.

PMID: 7832590 DOI: 10.1007/BF00872217.

Measurement and global analysis of the absorbance changes in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila.

Hoff W, van Stokkum I, van Ramesdonk H, van Brederode M, Brouwer A, Fitch J Biophys J. 1994; 67(4):1691-705.

PMID: 7819501 PMC: 1225531. DOI: 10.1016/S0006-3495(94)80643-5.

Photoinduced volume change and energy storage associated with the early transformations of the photoactive yellow protein from Ectothiorhodospira halophila.

van Brederode M, Gensch T, Hoff W, Hellingwerf K, Braslavsky S Biophys J. 1995; 68(3):1101-9.

PMID: 7756529 PMC: 1281832. DOI: 10.1016/S0006-3495(95)80284-5.

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