[29] N → O acyl rearrangement

Iwai, Koichi; Ando, Toshio

doi:10.1016/s0076-6879(67)11031-8

Cited by 74 publications

(47 citation statements)

References 40 publications

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“…Therefore sequence determination of residues 1-4 (Thr-Asp-Val-Glu) involved both subdigestion and deacylation of the a-amino group. Deacylation by acid treatment of T1C2, probably causing a N -O 0 shift of the blocking group from the a-amino to the hydroxyl of threonine-1 (24), produced some molecules with free amino termini and allowed the determination of residues [1][2][3][4][5][6][7] by Edman degradation (Fig. 3).…”

Section: Methodsmentioning

confidence: 99%

Amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase from rabbit skeletal muscle.

Scott

Fischer

Takio

et al. 1985

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

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The amino acid sequence of rabbit skeletal muscle heat-stable inhibitor of the cAMP-dependent protein kinase has been determined by microsequencing techniques. Proof of the structure involved a series of nonoverlapping tryptic fragments for primary identification of 86% of the amino acids. Complementary fragments generated by cleavage with chymotrypsin, Staphylococcus aureus V8 proteinase, and mast cell proteinase II contributed to proof of the structure. The inhibitor is a single polypeptide chain of 75 residues and has a molecular weight of 7829. It lacks tryptophan, proline, and sulfur-containing amino acids. The amino terminus of the inhibitor is blocked by an unidentified group. The aminoterminal region of the molecule contains the kinase inhibitory domain, and synthetic peptides based on the sequence of residues 11-30 are potent competitive inhibitors of the cAMPdependent protein kinase

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Section: Methodsmentioning

confidence: 99%

Amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase from rabbit skeletal muscle.

Scott

Fischer

Takio

et al. 1985

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

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“…The modified histone H1 was treated with hydroxylamine prior to digestion in order to hydrolyze 0-succinyl serine or threonine linkages. Smaller fragments were obtained by digestion with staphylococcal protease [17] (a gift of Dr G. Drapeau), chymotrypsin, thermolysin (a gift of Dr T. Ando) or by N + 0 acyl rearrangement [18].…”

Section: Fragmentation Of Histone H1mentioning

confidence: 99%

“…The presence of an amide at Asn-99 was deduced from the simultaneous appearance of both aspartic acid plus excess ammonia after hydriodic acid hydrolysis of the 2-anilinothiazolinone. In anhydrous acid the N-peptide bond of seryl and, to a lesser extent, of threonyl residues is known to undergo rearrangement to the hydroxyl group to form the O-acyl derivative [18]. This 0-peptide bond is much more labile to nucleophilic attack than the N-peptide bond and can theoretically be cleaved selectively and completely in acid or base with minimal N-peptide bond cleavage.…”

Section: Succinylated Chimentioning

confidence: 99%

The Amino-Acid Sequence of Trout-Testis Histone H1

1977

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The complete amino-acid sequence of 194 residues of trout testis histone H1 has been elucidated by automatic Edman degradation of large peptides derived from specific cleavages at infrequent amino-acid residues. Trout testis histone H1 has a molecular weight of 19314, is only slightly microheterogeneous, and possesses pentapeptide sequences related to Ala-Ah-Ala-Lys-Lys repeated six times in the complete sequence. Although the N-terminus of histone H1 is known to be blocked, some 10 of intact trout testis H1 contains a free N-terminal alanine residue. Three seryl residues in the C-terminal half of the molecule occur in the sequence Lys-Ser-Pro-Lys known to be phosphorylated in trout testis H1. The sequence has been compared to the known partial sequence of rabbit thymus H1. The results are consistent with a role for histone H1 in the maintenance of the higher-order structure of chromatin.

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“…It has been known since the 1960s that peptide bonds involving hydroxyl-containing residues can shift to ester bonds (NϾO acyl rearrangement) under laboratory conditions (35). There is now formal evidence that these reactions exist in several protein maturation pathways, including protein splicing (36), hedgehog protein maturation (32), pyruvoyl enzymes (37), and N-terminal nucleophile hydrolases (29,38) activations.…”

Section: Discussionmentioning

confidence: 99%

Self-catalyzed Cleavage of the Yeast Nucleoporin Nup145p Precursor

Teixeira

Fabre

Dujon³

1999

Journal of Biological Chemistry

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Nup145p is a component of the nuclear pore complex of Saccharomyces cerevisiae and is essential for mRNA export. Nup145p and its apparent vertebrate homologue are the only known nucleoporins to be composed of two functionally independent peptide moieties resulting from the post-translational cleavage of a large precursor molecule. In this study, the proteolytic cleavage site of Nup145p has been mapped upstream of an evolutionary conserved serine residue. Cleavage occurs at the same site when a precursor is artificially expressed in Escherichia coli. A hydroxyl-containing residue is critical for the reaction, although a thiol-containing residue offers an acceptable replacement. In vitro kinetics experiments using a purified precursor molecule demonstrate that the cleavage is self-catalyzed and that the catalytic domain lies within the N-terminal moiety. Taken altogether, our data are consistent with a proteolytic mechanism involving an N>O acyl rearrangement and a subsequent ester intermediate uncovered in other selfprocessing proteins.

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[29] N → O acyl rearrangement

Cited by 74 publications

References 40 publications

Amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase from rabbit skeletal muscle.

Amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase from rabbit skeletal muscle.

The Amino-Acid Sequence of Trout-Testis Histone H1

Self-catalyzed Cleavage of the Yeast Nucleoporin Nup145p Precursor

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