| Mutational and structural studies of the PixD BLUF output signal that affects light-regulated interactions with PixE. | |
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MedLine Citation:
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PMID: 21688827 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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PixD (Slr1694) is a BLUF (blue-light-using FAD) photoreceptor used by the cyanobacterium Synechocystis sp. PCC6803 to control phototaxis toward blue light. In this study, we probe the involvement of a conserved Tyr8-Gln50-Met93 triad in promoting an output signal upon blue light excitation of the bound flavin. Analysis of acrylamide quenching of Trp91 fluorescence shows that the side chain of this residue remains partially solvent exposed in both the lit and dark states. Mutational analysis demonstrates that substitution mutations at Tyr8 and Gln50 result in the loss of the photocycle while a mutation of Met93 does not appreciably disturb the formation of the light-excited state and only minimally accelerates its decay from 5.7 to 4.5 s. However, mutations of Tyr8, Gln50, and Met93 disrupt the ability of PixD dimers to interact with PixE to form a higher-order PixD(10)-PixE(5) complex, which is indicative of a lit conformational state. Solution nuclear magnetic resonance spectroscopy and X-ray crystallographic analyses confirm that a Tyr8 to Phe mutation is locked in a pseudo-light-excited state revealing flexible areas in PixD that likely constitute part of an output signal upon light excitation of wild-type PixD. |
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Authors:
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Hua Yuan; Vladimira Dragnea; Qiong Wu; Kevin H Gardner; Carl E Bauer |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2011-06-28 |
Journal Detail:
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Title: Biochemistry Volume: 50 ISSN: 1520-4995 ISO Abbreviation: Biochemistry Publication Date: 2011 Jul |
Date Detail:
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Created Date: 2011-07-19 Completed Date: 2011-09-19 Revised Date: 2011-09-26 |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 6365-75 Citation Subset: IM |
Copyright Information:
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© 2011 American Chemical Society |
Affiliation:
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Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405, USA. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/3MZI |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acrylamide Amino Acid Sequence Bacterial Proteins / chemistry*, genetics*, metabolism Chromatography, Gel Crystallography, X-Ray Darkness Flavin-Adenine Dinucleotide / metabolism* Fluorescence Light* Light Signal Transduction / radiation effects* Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Mutant Proteins / chemistry Mutation / genetics* Peptides / chemistry Photoreceptors, Microbial / chemistry*, genetics, metabolism Protein Binding / radiation effects Protein Structure, Tertiary Sequence Alignment Solvents Spectrophotometry, Ultraviolet Synechocystis / metabolism, radiation effects Tryptophan / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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GM40941/GM/NIGMS NIH HHS; R37 GM040941-24/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Mutant Proteins; 0/Peptides; 0/Photoreceptors, Microbial; 0/Solvents; 146-14-5/Flavin-Adenine Dinucleotide; 73-22-3/Tryptophan; 79-06-1/Acrylamide |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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