A cytoplasmic domain is required for the functional interaction of SRI and HtrI in archaeal signal transduction.

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 Lett

journal_title

FEBS letters

authors

Krah M,Marwan W,Oesterhelt D

doi

10.1016/0014-5793(94)01068-4

subject

Has Abstract

pub_date

1994-10-24 00:00:00

pages

301-4

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)01068-4

journal_volume

353

pub_type

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