Sequence Evidence for Strong Conservation of the Photoactive Yellow Proteins from the Halophilic Phototrophic Bacteria <i>Chromatium salexigens </i>and <i>Rhodospirillum salexigens</i>

Koh, Monjoo; Driessche, Gonzalez Van; Samyn, Bart; Hoff, Wouter D.; Meyer, Terry E.; Cusanovich, Michael A.; Beeumen, Jozef J. Van

doi:10.1021/bi951494t

Cited by 48 publications

(44 citation statements)

References 26 publications

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“…The highest sequence Shown are PAS domains from the DspA protein (sll0698) from Synechocystis sp. strain PCC 6803 (4); the YCF26 protein from a red algal chloroplast (40); the ResE (45) and the PhoR (27) proteins, both from Bacillus subtilis; the FixL protein from Rhizobium meliloti (16); the ArcB protein from E. coli (26); and the photoactive-yellow protein (PYP) from Halochromatium salexigens (29). The consensus sequence from a published alignment of PAS domains (54) is also shown (U, bulky hydrophobic: FILMVWY; h, hydrophobic: ILMV).…”

Section: Figmentioning

confidence: 99%

nblS, a Gene Involved in Controlling Photosynthesis-Related Gene Expression during High Light and Nutrient Stress inSynechococcus elongatusPCC 7942

2002

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The HliA protein of the cyanobacterium Synechococcus elongatus PCC 7942 is a small, thylakoid-associated protein that appears to play a role in photoprotection; its transcript rapidly accumulates in response to high-intensity light (HL) and the hli gene family is required for survival of cells in high light. In order to discover regulatory factors involved in HL acclimation in cyanobacteria, a screen was performed for chemically generated mutants unable to properly control expression of the hliA gene in response to HL. One such mutant was identified, and complementation analysis led to the identification of the affected gene, designated nblS. Based on its deduced protein sequence, NblS appears to be a membrane-bound, PAS-domain-bearing, sensor histidine kinase of two-component regulatory systems in bacteria. The nblS mutant was unable to properly control light intensity-mediated expression of several other photosynthesis-related genes, including all three psbA genes and the cpcBA genes. The mutant was also unable to control expression of the hliA and psbA genes in response to low-intensity blue/UV-A light, a response that may be related to the HL-mediated regulation of the genes. Additionally, in response to nutrient deprivation, the nblS mutant was unable to properly control accumulation of the nblA transcript and associated degradation of the light-harvesting phycobilisomes. The nblS mutant dies more rapidly than wild-type cells following exposure to HL or nutrient deprivation, likely due to its inability to properly acclimate to these stress conditions. Thus, the NblS protein is involved in the control of a number of processes critical for altering the photosynthetic apparatus in response to both HL and nutrient stress conditions.

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Section: Figmentioning

confidence: 99%

nblS, a Gene Involved in Controlling Photosynthesis-Related Gene Expression during High Light and Nutrient Stress inSynechococcus elongatusPCC 7942

2002

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“…6). 25 Enhanced conservation of the amino acid residues found in Table II may indicate that one or several of these residues play an important role for PYP function common to the different species.…”

Section: Specification Of Amino Acid Residues Showing Strong Sensitivmentioning

confidence: 99%

Molecular dynamics study of femtosecond events in photoactive yellow protein after photoexcitation of the chromophore

1998

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Molecular dynamics simulations were carried out to study what happens in a photoreceptor protein, photoactive yellow protein (PYP), immediately after the vertical transition of the chromophore from the ground to the excited state. A photon absorption simulation was performed to investigate the movement of amino acid residues upon photoexcitation. To calculate the excited state of the chromophore, SCF-CI calculation was carried out with INDO/S Hamiltonian. We observed that some amino acid residues have strong interactions with the chromophore. Most of these amino acid residues are conserved in PYPs from three different species of bacteria. This observation indicates the biological importance of these residues.

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“…PYP belongs to the novel group of photoreceptor proteins (3,4) whose structures are quite different from those of the other photoreceptor proteins studied so far. Namely, the protein moiety of PYP has an ␣/␤ fold structure (5) composed of 125 amino acids (6,7).…”

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confidence: 99%

Evidence for Proton Transfer from Glu-46 to the Chromophore during the Photocycle of Photoactive Yellow Protein

Imamoto

Mihara

Hisatomi

et al. 1997

Journal of Biological Chemistry

125

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Photoactive yellow protein (PYP) belongs to the novel group of eubacterial photoreceptor proteins. To fully understand its light signal transduction mechanisms, elucidation of the intramolecular pathway of the internal proton is indispensable because it closely correlates with the changes in the hydrogen-bonding network, which is likely to induce the conformational changes. For this purpose, the vibrational modes of PYP and its photoproduct were studied by Fourier transform infrared spectroscopy at ؊40°C. The vibrational modes characteristic for the anionic p-coumaryl chromophore (Kim, M., Mathies, R. A., Hoff, W. D., and Hellingwerf, K. J. (1995) Biochemistry 34, 12669 -12672) were observed at 1482, 1437, and 1163 cm ؊1 for PYP. However, the bands corresponding to these modes were not observed for PYP M , the blue-shifted intermediate, but the 1175 cm ؊1 band characteristic of the neutral p-coumaryl chromophore was observed, indicating that the phenolic oxygen of the chromophore is protonated in PYP M . A 1736 cm ؊1 band was observed for PYP, but the corresponding band for PYP M was not. Because it disappeared in the Glu-46 3 Gln mutant of PYP, this band was assigned to the C‫؍‬O stretching mode of the COOH group of Glu-46. These results strongly suggest that the proton at Glu-46 is transferred to the chromophore during the photoconversion from PYP to PYP M .Photoactive yellow protein (PYP) 1 ( max ϭ 446 nm) (1) is proposed to be a photoreceptor protein for the negative phototaxis observed in the purple phototrophic bacterium, Ectothiorhodospira halophila (2). PYP belongs to the novel group of photoreceptor proteins (3, 4) whose structures are quite different from those of the other photoreceptor proteins studied so far. Namely, the protein moiety of PYP has an ␣/␤ fold structure (5) composed of 125 amino acids (6, 7). The chromophore is a p-coumaric acid (7-9) bound to a cysteine residue via a thioester bond.PYP absorbs a photon and enters the photocycle. We have analyzed the photocycle of PYP in detail by low temperature spectroscopy and identified several intermediates (10). Irradiation of PYP at Ϫ190°C yields PYP B ( max ϭ 489 nm) and PYP H ( max ϭ 442 nm), which are thermally converted to PYP L ( max ϭ 456 nm) through PYP BL ( max ϭ 400 nm) and PYP HL ( max ϭ 447 nm), respectively. The two pathways beginning with PYP B and PYP H join at PYP L and revert to PYP. Flash photolysis at ambient temperature identified two intermediates, pR ( max ϭ 465 nm) and pB ( max ϭ 355 nm) (11,12). pR is formed within 10 ns after flash excitation. It decays to pB over a submillisecond time scale and reverts to PYP within 1 s. It has been demonstrated that pR is the same species as PYP L (10) (In this paper, pR and pB are called PYP L and PYP M , respectively, to avoid confusion) and that PYP L is accumulated by irradiation of PYP at Ϫ80°C (10, 13). However, the precursors of PYP L have not been discovered by flash photolysis at room temperature.Recent studies have clarified some details of the events that take place during t...

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Sequence Evidence for Strong Conservation of the Photoactive Yellow Proteins from the Halophilic Phototrophic Bacteria Chromatium salexigens and Rhodospirillum salexigens

Cited by 48 publications

References 26 publications

nblS, a Gene Involved in Controlling Photosynthesis-Related Gene Expression during High Light and Nutrient Stress inSynechococcus elongatusPCC 7942

nblS, a Gene Involved in Controlling Photosynthesis-Related Gene Expression during High Light and Nutrient Stress inSynechococcus elongatusPCC 7942

Molecular dynamics study of femtosecond events in photoactive yellow protein after photoexcitation of the chromophore

Evidence for Proton Transfer from Glu-46 to the Chromophore during the Photocycle of Photoactive Yellow Protein

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