Abstract:
:Phototaxis in the archaeon Halobacterium salinarium is mediated by a stable complex of the photoreceptor sensory rhodopsin I and its transducer HtrI, which relays the light stimulus to the signalling pathway. Removal of the cytoplasmic signalling domain of HtrI eliminated the SRI-specific motor response to light stimulation and led to the loss of the spectroscopically detectable physical interaction of SRI and HtrI. A similar phenotype was obtained by deleting part of a cytoplasmic loop located between the second transmembrane helix of HtrI and the signalling domain. These results indicate that the photochemical behavior of sensory rhodopsin I is not determined by interaction with the transmembrane helices of HtrI per se but functionally coupled to the signalling domain. It is proposed that light excitation of SRI results in a conformational change of the transducer which is conducted by the cytoplasmic loop, an extra module not found in the eubacterial transducer homologues, and activates the signalling domain.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Krah M,Marwan W,Oesterhelt Ddoi
10.1016/0014-5793(94)01068-4subject
Has Abstractpub_date
1994-10-24 00:00:00pages
301-4issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(94)01068-4journal_volume
353pub_type
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