Sequence variability in the retinal-attachment domain of mammalian rhodopsins

Pappin, Darryl; Findlay, John B. C.

doi:10.1042/bj2170605

Cited by 41 publications

(15 citation statements)

References 31 publications

(35 reference statements)

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“…These changes appear to involve distortion of a local residues which are not highly conserved in this region are the Ones immediately following the lysine but these still show 'size-conservation'. Further, this segment (residues 290-302) does not have a high grave et d., 1983;Pappin and Findlay, 1984) and thus might easily switch between conformations. By the meta I stage, the protein undergoes further conformational changes which appear to involve ahelical domains.…”

Section: Phospholipid Alterationsmentioning

confidence: 99%

Photoexcitation of Rhodopsin: Conformation Changes in the Chromophore, Protein and Associated Lipids as Determined by Ftir Difference Spectroscopy

DeGrip¹,

Gray²,

Gillespie³

et al. 1988

Photochem & Photobiology

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Abstract— The visual pigment rhodopsin is the major membrane protein in the rod photoreceptor membrane. Rhodopsin's function is to transduce the light induced isomerization (ll‐cis to all‐trans) of its internally located retinylidene chromophore into transient expression of signal sites at the surface of the protein. Fourier transform infrared (FTIR) difference spectroscopy has been used to study all of the steps in the photobleaching sequence of rhodopsin. Early protein alterations involving the peptide backbone and aspartic and/or glutamic carboxyl groups were detected which increase upon lumirhodopsin formation and spread to water exposed carboxyl groups by metarhodopsin II. The intensified and frequency shifted hydrogen‐out‐of‐plane vibrations of the chromophore that are present in bathorhodopsin are absent in lumirhodopsin. This indicates that by lumirhodopsin, the chromophore has relaxed relative to its more strained all‐frans form in bathorhodopsin. Finally, the transition to metarhodopsin II is found to involve perturbation of the acyl tail region of unsaturated phospholipid molecules possibly in response to small changes in the shape of the rhodopsin.

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Section: Phospholipid Alterationsmentioning

confidence: 99%

Photoexcitation of Rhodopsin: Conformation Changes in the Chromophore, Protein and Associated Lipids as Determined by Ftir Difference Spectroscopy

DeGrip¹,

Gray²,

Gillespie³

et al. 1988

Photochem & Photobiology

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“…Attachment yields were monitored by radioactivity. The glass-coupled polypeptide was then sequenced by automated solid-phase Edman degradation (Laursen, 1971) (Pappin and Findlay, 1984), 3 min wash with methanol (2 ml/min), 3 min wash with benzene (2 ml/min). followed by 5 min cleavage with anhydrous trifluoroacetic acid (TFA) (0.2 ml/min).…”

Section: Sds-polyacrylamide Gel Electrophoresis (Sds-page) Electroelmentioning

confidence: 99%

Coronavirus IBV: Partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41

Cavanagh¹,

Davis²,

et al. 1986

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The spike protein of avian infectious bronchitis coronavirus comprises two glycopolypeptides S1 and S2 derived by cleavage of a proglycopolypeptide So, the nucleotide sequence of which has recently been determined for the Beaudette strain (Binns, M.M. et al., 1985, J. Gen. Virol. 66, 719-726). The order of the two glycopolypeptides within So is aminoterminus(N)-S1-S2-carboxyterminus(C). To locate the N-terminus of S2 we have performed partial amino acid sequencing on S2 from IBV-Beaudette labelled with [3H]serine and from the related strain labelled with [3H]valine, leucine and isoleucine. The residues identified and their positions relative to the N-terminus of S2 were: serine, 13; valine, 6, 12; leucine, none in the first 20 residues; isoleucine, 2, 19. These results identified the N-terminus of S2 of IBV-Beaudette as serine, 520 residues from the N-terminus of S1, excluding the signal sequence. Immediately to the N-terminal side of residue 520 So has the sequence Arg-Arg-Phe-Arg-Arg; similar basic connecting peptides are a feature of several other virus spike glycoproteins. It was deduced that for IBV-Beaudette S1 comprises 519 residues (Mr 57.0K) or 514 residues (56.2K) if the connecting peptide was to be removed by carboxypeptidase-like activity in vivo while S2 has 625 residues (69.2K). Nucleotide sequencing of the cleavage region of the So gene of IBV-M41 revealed the same connecting peptide as IBV-Beaudette and that the first 20 N-terminal residues of S2 of IBV-M41 were identical to those of the Beaudette strain. IBV-Beaudette grown in Vero cells had some uncleaved So; this was cleavable by 10 micrograms/ml of trypsin and of chymotrypsin. Partial N-terminal analysis of S1 from IBV-M41 identified leucine and valine residues at positions 2 and 9 respectively from the N-terminus. This confirms the identification, made by Binns et al. (1985), of the N-terminus of S1 and the end of the signal sequence of the IBV-Beaudette spike propolypeptide. N-terminal sequencing of [3H]leucine-labelled IBV-Beaudette membrane (M) polypeptide showed leucine residues at positions 8, 16 and 22 from the N-terminus; these results confirm the open reading frame identified by M.E.G. Boursnell et al. (1984, Virus Res. 1, 303-313) in the nucleotide sequence of M. The N-terminus of the nucleocapsid (N) polypeptide appeared to be blocked.

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“…Proteolytic cleavage of the wild-type HoxH protein was conducted with endoproteinase Glu-C (Boehringer Mannheim) at 25ЊC for 18 h in 25 mM ammonium carbonate buffer (pH 8.0) containing 5% acetonitrile. The digestion mixture contained 400 g of HoxH protein and 20 g of endoproteinase Glu-C in a final volume of 400 l. The HoxH precursor was cleaved with CNBr as described previously (11,24). A 400-g portion of protein was resolved in 400 l of 70% formic acid, 20 l of a CNBr stock solution in acetonitrile (100 mg/ml) was added, and the reaction mixture was flushed with N 2 and incubated at 25ЊC for 24 h in the dark.…”

Section: Methodsmentioning

confidence: 99%

Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrophus requires the hoxW gene product

et al. 1996

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Two open reading frames (ORFs) were identified immediately downstream of the four structural genes for the soluble hydrogenase (SH) of Alcaligenes eutrophus H16. While a mutation in ORF2 had no obvious effect on hydrogen metabolism, an in-frame deletion in ORF1, subsequently designated hoxW, led to a complete loss of SH activity and hence a significant retardation of autotrophic growth on hydrogen. Hydrogen oxidation in the hoxW mutant was catalyzed by the second hydrogenase, a membrane-bound enzyme. Assembly of the four subunits of the SH was blocked in mutant cells, and HoxH, the hydrogen-activating subunit, accumulated as a precursor which was still capable of binding nickel. Protein sequencing revealed that HoxH isolated from the wild type terminates at His-464, whereas the C-terminal amino acid sequence of HoxH from the hoxW mutant is colinear with the deduced sequence. Processing of the HoxH precursor was restored in vitro by a cell extract containing HoxW. These results indicate that HoxW is a highly specific carboxyl-terminal protease which releases a 24-amino-acid peptide from HoxH prior to progression of subunit assembly.The facultative lithoautotroph Alcaligenes eutrophus can use molecular hydrogen as the sole energy source. Hydrogen oxidation in this proteobacterium is mediated by two (NiFe)-containing hydrogenases. The membrane-bound hydrogenase (MBH) is composed of a large and a small subunit, which are coupled to electron transport phosphorylation via a cytochrome b-like anchor protein. While the MBH is a representative of the more common type of (NiFe)-hydrogenases, the second, soluble hydrogenase (SH) belongs to a family of less abundant multimeric (NiFe)-hydrogenases (reviewed in reference 7). Multimeric hydrogenases are present in a few Alcaligenes species, in the gram-positive Rhodococcus sp. strain 1b (formerly Nocardia opaca) (4), and in the cyanobacterium Anabaena variabilis (32).The cytoplasmic SH reacts with NAD as the physiological electron carrier. The enzyme is composed of four heterologous subunits (35) encoded by the megaplasmid-borne genes hoxF, hoxU, hoxY, and hoxH (39). The products of hoxF and hoxU form the flavononheme iron protein of the SH which possesses NADH oxidoreductase (diaphorase) activity (33). The diaphorase dimer is closely related to three peripheral subunits of the NADH:ubiquinone oxidoreductase (complex I) of mitochondria and of some bacterial species (42, 43). The hoxH and hoxY gene products show features of a hydrogen-activating site and an intramolecular electron transfer pathway (7). The first crystallographic analysis of a (NiFe)-hydrogenase carried out for the periplasmic hydrogenase of Desulfovibrio gigas was recently completed. According to this study, the active site appears to be a binuclear cluster of nickel and probably iron, buried deep inside the protein (41).Genetic studies on various bacteria uncovered a series of accessory genes which code for functions involved in the biogenesis of (NiFe)-hydrogenases. Several specific gene products are required...

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Sequence variability in the retinal-attachment domain of mammalian rhodopsins

Abstract: Ovine rhodopsin was regenerated with 11-cis-[15-3H]

Cited by 41 publications

References 31 publications

Photoexcitation of Rhodopsin: Conformation Changes in the Chromophore, Protein and Associated Lipids as Determined by Ftir Difference Spectroscopy

Photoexcitation of Rhodopsin: Conformation Changes in the Chromophore, Protein and Associated Lipids as Determined by Ftir Difference Spectroscopy

Coronavirus IBV: Partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41

Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrophus requires the hoxW gene product

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