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J. Biol. Chem., Vol. 269, Issue 31, 19738-19744, 08, 1994
A Anukanth and HG Khorana
We concluded previously from mutagenesis in the intradiscal domain of
bovine rhodopsin that the formation of a tertiary structure comprising the
N-terminal tail and the three polypeptide loops is essential to the in vivo
assembly of the functional rhodopsin. We now report on more comprehensive
mutagenic studies in the intradiscal domain to determine more precisely the
requirement for the formation of the above-proposed tertiary structure.
Three large deletions, two consisting of groups of 10 amino acids each, and
the third of 34 amino acids, were carried out in the N-terminal loop. All
the three mutant opsins only poorly formed the rhodopsin chromophore. In
the BC loop, we carried out five 2 amino acid deletions, 2 single amino
acid deletions, and three mutations in which short sequences in the loop
were reversed. All the resulting mutant opsins had lost the ability to bind
11-cis-retinal. In the DE loop, where extensive mutagenesis had previously
been carried out, we carried out 3 amino acid replacements (Asn, Thr, Tyr)
at Cys187. None of these mutants bound 11-cis-retinal. In loop FG, we
carried out four 2 amino acid deletions, 1 single amino acid deletion, 3
amino acid replacements, and one mutation in which the sequence of the 7
amino acids was reversed. All the mutants in FG loop partially formed the
rhodopsin chromophore. All the mutants now described appeared to be
retained in the endoplasmic reticulum: several that were examined in detail
were complexed with non-opsin proteins, the chaperonins. Treatment with
ATP-MgCl2 released the latter from the mutant rhodopsins. Our overall
conclusion is that the formation of the specific structure in the
intradiscal domain has highly stringent spatial requirements.
Structure and function in rhodopsin. Requirements of a specific structure for the intradiscal domain
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
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