Home > Publications database > Shape and oligomerization state of the cytoplasmic domain of the phototaxis transducer II from Natronobacterium pharaonis > print

001     53707
005     20250129094226.0
017 _ _ |a This version is available at http://www.pnas.org, http://dx.doi.org/10.1073/pnas.0607201103
024 7 _ |2 pmid
|a pmid:17032755
024 7 _ |2 pmc
|a pmc:PMC1592645
024 7 _ |2 DOI
|a 10.1073/pnas.0607201103
024 7 _ |2 WOS
|a WOS:000241476200029
024 7 _ |2 Handle
|a 2128/2656
037 _ _ |a PreJuSER-53707
041 _ _ |a eng
082 _ _ |a 000
084 _ _ |2 WoS
|a Multidisciplinary Sciences
100 1 _ |0 P:(DE-HGF)0
|a Budyak, I. L.
|b 0
245 _ _ |a Shape and oligomerization state of the cytoplasmic domain of the phototaxis transducer II from Natronobacterium pharaonis
260 _ _ |a Washington, DC
|b Academy
|c 2006
300 _ _ |a 15428 - 15433
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 5100
|a Proceedings of the National Academy of Sciences of the United States of America
|v 103
|x 0027-8424
|y 42
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Phototaxis allows archaea to adjust flagellar motion in response to light. In the photophobic response of Natronobacterium pharaonis, light-activated sensory rhodopsin II causes conformational changes in the transducer II protein (pHtrII), initiating the two-component signaling system analogous to bacterial chemotaxis. pHtrII's cytoplasmic domain (pHtrII-cyt) is homologous to the cytoplasmic domains of eubacterial chemotaxis receptors. Chemotaxis receptors require dimerization for activity and are in vivo-organized in large clusters. In this study we investigated the oligomerization and aggregation states of pHtrII-cyt by using chemical cross-linking, analytical gel-filtration chromatography, and small-angle neutron scattering. We show that pHtrII-cyt is monomeric in dilute buffers, but forms dimers in 4 M KCl, the physiological salt concentration for halophilic archaea. At high ammonium sulfate concentration, the protein forms higher-order aggregates. The monomeric protein has a rod-like shape, 202 A in length and 14.4 A in diameter; upon dimerization the length increases to 248 A and the diameter to 18.2 A. These results suggest that under high salt concentration the shape and oligomerization state of pHtrII-cyt are comparable to those of chemotaxis receptors.
536 _ _ |0 G:(DE-Juel1)FUEK409
|2 G:(DE-HGF)
|a Funktion und Dysfunktion des Nervensystems
|c P33
|x 0
536 _ _ |0 G:(DE-Juel1)FUEK414
|a Kondensierte Materie
|c P54
|x 1
536 _ _ |0 G:(DE-Juel1)FUEK415
|a Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)
|c P55
|x 2
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Archaeal Proteins: chemistry
650 _ 2 |2 MeSH
|a Archaeal Proteins: genetics
650 _ 2 |2 MeSH
|a Archaeal Proteins: metabolism
650 _ 2 |2 MeSH
|a Biopolymers: chemistry
650 _ 2 |2 MeSH
|a Carotenoids: chemistry
650 _ 2 |2 MeSH
|a Carotenoids: genetics
650 _ 2 |2 MeSH
|a Carotenoids: metabolism
650 _ 2 |2 MeSH
|a Cross-Linking Reagents: chemistry
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Dimerization
650 _ 2 |2 MeSH
|a Light
650 _ 2 |2 MeSH
|a Natronobacterium: chemistry
650 _ 2 |2 MeSH
|a Natronobacterium: metabolism
650 _ 2 |2 MeSH
|a Particle Size
650 _ 2 |2 MeSH
|a Phototrophic Processes: physiology
650 _ 2 |2 MeSH
|a Protein Structure, Quaternary
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 7 |0 0
|2 NLM Chemicals
|a Archaeal Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Biopolymers
650 _ 7 |0 0
|2 NLM Chemicals
|a Cross-Linking Reagents
650 _ 7 |0 0
|2 NLM Chemicals
|a phototaxis receptor sensory rhodopsin II, Natronobacterium pharaonis
650 _ 7 |0 36-88-4
|2 NLM Chemicals
|a Carotenoids
650 _ 7 |2 WoSType
|a J
653 2 0 |2 Author
|a archaebacteria
653 2 0 |2 Author
|a dynamics
653 2 0 |2 Author
|a halophilic
653 2 0 |2 Author
|a small-angle neutron scattering
700 1 _ |0 P:(DE-Juel1)VDB4339
|a Pipich, V.
|b 1
|u FZJ
700 1 _ |0 P:(DE-HGF)0
|a Mironova, O. S.
|b 2
700 1 _ |0 P:(DE-HGF)0
|a Schlesinger, R.
|b 3
700 1 _ |0 P:(DE-HGF)0
|a Zaccai, G.
|b 4
700 1 _ |0 P:(DE-HGF)0
|a Klein-Seetharaman, J.
|b 5
773 _ _ |0 PERI:(DE-600)1461794-8
|a 10.1073/pnas.0607201103
|g Vol. 103, p. 15428 - 15433
|p 15428 - 15433
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|t Proceedings of the National Academy of Sciences of the United States of America
|v 103
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|y 2006
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1592645
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