PMID- 17655327
OWN - NLM
STAT- MEDLINE
DCOM- 20071009
LR  - 20070816
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 46
IP  - 33
DP  - 2007 Aug 21
TI  - FT-IR difference spectroscopy elucidates crucial interactions of sensory 
      rhodopsin I with the cognate transducer HtrI.
PG  - 9399-405
AB  - The phototaxis receptor sensory rhodopsin I (SRI) from Halobacterium salinarum 
      interacts with its cognate transducer (HtrI) forming a transmembrane complex. 
      After light excitation of the chromophore all-trans retinal, SRI undergoes 
      structural changes that are ultimately transmitted to HtrI. The interaction of 
      SRI with HtrI results in the closure of the receptor's proton pathway, which 
      renders the photocycle recovery kinetics of SRI pH-independent. We demonstrate on 
      heterologously expressed and reconstituted SRI-HtrI fusion proteins that the 
      transmembrane part of HtrI (residues 1-52) as well as the downstream cytoplasmic 
      part (residues 53-147) exhibit conformational changes after light excitation. The 
      sum of these conformational changes is similar to those observed in the fusion 
      constructs SRI-HtrI 1-71 and SRI-HtrI 1-147, which display pH-independent 
      receptor kinetics. These results indicate the occurrence of spatially distinct 
      conformational changes that are required for functional signal transmission. 
      Kinetic and spectroscopic analysis of HtrI point mutants of Asn53 provides 
      evidence that this residue is involved in the receptor-transducer interaction. We 
      suggest that Asn53 plays a role similar to that of Asn74 of the HtrII from 
      Natronobacterium pharaonis, the latter forming a hydrogen bond to the receptor 
      within the membrane.
FAU - Mironova, Olga S
AU  - Mironova OS
AD  - Research Center Julich, Institute for Structural Biology (IBI-2), 52425 Julich, 
      Germany.
FAU - Budyak, Ivan L
AU  - Budyak IL
FAU - Buldt, Georg
AU  - Buldt G
FAU - Schlesinger, Ramona
AU  - Schlesinger R
FAU - Heberle, Joachim
AU  - Heberle J
LA  - eng
PT  - Journal Article
DEP - 20070727
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Archaeal Proteins)
RN  - 0 (Halorhodopsins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (SRI protein, Halobacterium)
RN  - 0 (Sensory Rhodopsins)
RN  - 0 (htrI protein, Halobacterium salinarium)
RN  - 7006-34-0 (Asparagine)
SB  - IM
MH  - Archaeal Proteins/*chemistry/genetics/radiation effects
MH  - Asparagine/chemistry/genetics
MH  - Halorhodopsins/*chemistry/genetics/radiation effects
MH  - Light
MH  - Membrane Proteins/*chemistry/genetics/radiation effects
MH  - Point Mutation
MH  - Protein Interaction Mapping
MH  - Recombinant Fusion Proteins/chemistry/genetics/radiation effects
MH  - Sensory Rhodopsins/*chemistry/genetics/radiation effects
MH  - Spectroscopy, Fourier Transform Infrared
EDAT- 2007/07/28 09:00
MHDA- 2007/10/10 09:00
CRDT- 2007/07/28 09:00
PHST- 2007/07/28 09:00 [pubmed]
PHST- 2007/10/10 09:00 [medline]
PHST- 2007/07/28 09:00 [entrez]
AID - 10.1021/bi700563f [doi]
PST - ppublish
SO  - Biochemistry. 2007 Aug 21;46(33):9399-405. doi: 10.1021/bi700563f. Epub 2007 Jul 
      27.