Amino acid sequences of α-helical segments from <i>S</i>-carboxymethylkerateine-A. Complete sequence of a type-II segment

Crewther, W.G.; Inglis, A.S.; McKern, Neil M.

doi:10.1042/bj1730365

Cited by 64 publications

(37 citation statements)

References 31 publications

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“…Residue numbers and sequences are from Fig. 1 (25) and is indicative of a coiled-coil conformation. Screening the sequences of the isolated helical segment ofkerateine-A (25) and rabbit muscle tropomyosin (26), which is another highly a-helical molecule with coiled-coil structure (24-28), we noticed a closely related sequence (Fig.…”

Section: Discussionmentioning

confidence: 99%

Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin.

Geisler¹,

Weber²

1981

Proc. Natl. Acad. Sci. U.S.A.

140

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Although all intermediate-sized filaments (10-nm filaments) seem to show similar morphology and share a number of biochemical properties, different cell-and tissue-specific subclasses have been distinguished by immunological experiments and by differences in apparent molecular weights and isoelectric points of the major constituent proteins. In order to understand the degree of possible homology between these proteins, we have begun amino acid sequence analysis of the polypeptides. Here we characterize a large fragment of chicken gizzard and pig stomach desmin as well as the corresponding fragment from porcine eye lens vimentin. The fragments are situated at the carboxyl end and consist of 138-140 amino acid residues-i.e., some 28% ofthe corresponding polypeptide chains. The results show that the two immunologically distinct porcine-proteins are. different gene products. They show a related amino acid sequence but differ in 36% of the residues present in the carboxy-terminal part. In contrast the two desmins, although from species as diverse as chicken and pig, are more closely related and differ in less than 9% of the residues in the corresponding carboxy-terminal region. Thus tissue specificity overrides species divergence. These results are discussed in the light of previous immunological experiments. They lend further support to the hypothesis that intermediate filaments belong to a multigene family, which is expressed in line with certain rules of differentiation during embryogenesis.Intermediate-sized or 7-to 10-nm filaments form one of the three major components of the cytoskeleton. (5,6).In spite of the differences revealed by two-dimensional gel analysis and the lack of immunological crossreactivity experienced with many antibodies, the structural proteins of these filaments share several distinct properties. The filaments show a very similar ultrastructure and morphology and belong to the highly helical k-m-e-f-type ofproteins (see, for instance, ref. 7). In addition they are all insoluble in physiological buffers (for references see above) and, with the exception of certain neurofilament proteins, contain polypeptides of molecular weights in the range 45,000-68,000 (for references see refs. 1 and 2).In order to see whether different intermediate filament proteins are related in primary structure, we have started a comparative protein-chemical study based on partial amino acid sequence analysis. We chose stomach as the source of desmin, because it is generally the tissue of choice for the purification of this type of intermediate filament (1). In addition we have used eye lens fiber tissue as the source of an intermediate filament polypeptide distinct by apparent polypeptide molecular weight and isoelectric point. This protein has been immunologically and electrophoretically characterized (8) as related to the vimentin-type filaments typically expressed in fibroblasts and other mesenchymally derived cells as well as in most cultured cells (for references see refs. 1-4).Here we show that cleav...

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Section: Discussionmentioning

confidence: 99%

Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin.

Geisler¹,

Weber²

1981

Proc. Natl. Acad. Sci. U.S.A.

140

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“…Some evidence for the formation of succinic anhydride in a protein context was suggested to occur in insulin A-chain C-terminal Asn (23). The observation of protein cleavage after aspartic residues, when exposed to dilute HCl or formic acid (pH 2) and high temperature (108°C) (24), led to the suggestion that the intermediate, formed after Asp exposure to these conditions, is a succinic anhydride. Once formed, it allows the cleavage between Asp and adjacent amino acid.…”

Section: Fig 6 Alternative Reactions For Resolving the Branched Intmentioning

confidence: 99%

Protein Splicing of Inteins with Atypical Glutamine and Aspartate C-terminal Residues

Amitai

Dassa

Pietrokovski

2004

Journal of Biological Chemistry

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Inteins are protein-splicing domains present in many proteins. They self-catalyze their excision from the host protein, ligating their former flanks by a peptide bond. The C-terminal residue of inteins is typically an asparagine (Asn). Cyclization of this residue to succinimide causes the final detachment of inteins from their hosts. We studied protein-splicing activity of two inteins with atypical C-terminal residues. One having a C-terminal glutamine (Gln), isolated from Chilo iridescent virus (CIV), and another unique intein, first reported here, with a C-terminal aspartate, isolated from Carboxydothermus hydrogenoformans (Chy). Protein-splicing activity was examined in the wild-type inteins and in several mutants with N-and C-terminal amino acid substitutions. We demonstrate that both wild-type inteins can protein splice, probably by new variations of the typical protein-splicing mechanism. Substituting the atypical C-terminal residue to the typical Asn retained protein-splicing only in the CIV intein. All diverse C-terminal substitutions in the Chy intein (Asp 345 to Asn, Gln, Glu, and Ala) abolished protein-splicing and generated N-and C-terminal cleavage. The observed Cterminal cleavage in the Chy intein ending with Ala cannot be explained by cyclization of this residue. We present and discuss several new models for reactions in the protein-splicing pathway.Inteins are proteins that catalyze their own excision out of diverse host proteins while ligating the polypeptide flanks (Nextein and C-extein) of their host protein. This process, termed protein-splicing, is an intramolecular event, not requiring additional enzymes. Protein-splicing, as currently understood, requires four successive steps, directly involving three conserved intein positions: (i) Cys or Ser at the N terminus of the intein; (ii) Asn at the intein C terminus; and (iii) Cys, Ser, or Thr directly following the intein C terminus (1, 2). Few inteins with an N-terminal Ala residue differ in the first step of the reaction and have been described (3).Protein-splicing typically commences by an N 3 O or N 3 S acyl rearrangement of the peptide bond between the N-extein and the N terminus of the intein into an ester intermediate. This step involves the nucleophilic attack of the thiol or hydroxyl side chain of the intein N-terminal amino acid (Cys or Ser, respectively) on the carbonyl group of the adjacent Nextein peptide bond (4). Instantaneously, the thiol or hydroxyl, of the residue following the intein C terminus, attacks the ester bond. In inteins with N-terminal Ala residues, the N-terminal peptide bond is not rearranged by the N-terminal Ala but by the nucleophilic group of the residue immediately following the intein C terminus (3). In either case, a branched intermediate is formed: the N-extein is connected by an ester bond to the side chain of the first C-extein residue, whereas this residue is also connected by a peptide bond to the intein C terminus (5, 6) ( Fig.

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“…Determination of the sizes of the presumably small domains 1 and 5 will have to await amino acid sequence analyses. It is noteworthy that the a-helical sections of wool keratin filaments are also A long and ;12,000 in Mr (27)(28)(29) The three-chain coiled-coil a-helical segments (t180 A long) correspond to particle 2, and the region containing both segments (-400 A long) corresponds to particle 1. Thus, the non-a-helix of domain 3 is -40 A long and that of domains 1 plus 5 to 7 is perhaps %80 A long.…”

Section: Isolation and Characterization Of A-helix-enrichedmentioning

confidence: 99%

Intermediate filaments of baby hamster kidney (BHK-21) cells and bovine epidermal keratinocytes have similar ultrastructures and subunit domain structures.

Steinert¹,

Idler²,

Goldman³

1980

Proc. Natl. Acad. Sci. U.S.A.

125

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structurally identical a-helix-enriched particles were released. Their properties indicated these IF were composed of a similar threechain unit which contained regions of coiled-coil a-helix interspersed with regions of non-a-helix. These two types of experiments permited the construction of subunit domain maps which revealed a common structure: all subunits possessed two a-helical domains of the same size that were adjoined by non-a-helical domains of variable size. We propose that the reported solubility and immunological differences in these IF and perhaps those of other types of cells are due largely to variations in the size, configuration, and amino acid sequence of the nona-helical regions of the subunits in the IF.

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Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment

Cited by 64 publications

References 31 publications

Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin.

Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin.

Protein Splicing of Inteins with Atypical Glutamine and Aspartate C-terminal Residues

Intermediate filaments of baby hamster kidney (BHK-21) cells and bovine epidermal keratinocytes have similar ultrastructures and subunit domain structures.

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