Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia

G. T. Nagle, S. D. Painter, J. E. Blankenship, J. D. Dixon, A. Kurosky

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

Three peptide complexes which can induce egg laying in Aplysia were isolated from the atrial gland of the marine mollusc Aplysia californica and chemically characterized. Amino acid sequence analyses established the covalent structures, including disulfide assignments, of all three dimeric complexes. Each complex consisted of an identical 18-residue peptide (A-AP) which was disulfide-bonded to a 36-residue peptide that was homologous to bag cell egg-laying hormone (EHL). The primary structure of A-AP was determined to be: NH2-Asp-Ser-Asp-Val-Ser-Leu-Phe-Asn-Gly-Asp-Leu-Leu-Pro-Asn -Gly-Arg-Cys-Ser-COOH. The primary structure of one of the three ELH-regulated peptides (A-ELH) was determined to be NH2-Ile-Ser-Ile-Asn-Gln-Asp-Leu-Lys-Ala-Ile-Thr-Asp-Met-Leu -Leu-Thr-Glu-Gln-Ile-Gln-Ala-Arg-Arg-Arg-Cys-Leu-Asp-Ala-Leu -Arg-Gln-Arg-Leu-Leu-Asp-Leu-COOH. The two ELH-related peptides, [Ala27]A-ELH and [Gln23, Ala27]A-ELH, differed from A-ELH at 1 and 2 residues, respectively. Both [Ala27]A-ELH and [Gln23, Ala27]A-ELH were novel peptide sequences representing products of as yet uncharacterized genes within the ELH family. These structural studies provide the first direct chemical evidence that (a) an 18-residue peptide (A-AP) derived from a polypeptide precursor encoded by the A gene, as predicted from nucleotide sequence analysis, occurs in the atrial gland; (b) the Cys17 residue of A-AP is disulfide-bonded to Cys25 of A-ELH; and (c) A-AP also occurs disulfide-bonded to two additional, previously undescribed ELH-related peptides, [Ala27]A-ELH and [Gln23, Ala27]A-ELH.

Original languageEnglish (US)
Pages (from-to)7853-7859
Number of pages7
JournalJournal of Biological Chemistry
Volume261
Issue number17
StatePublished - 1986
Externally publishedYes

Fingerprint

Aplysia
Gene encoding
Ovum
Gene Expression
Peptides
Disulfides
antiarrhythmic peptide
Genes
Molluscs
Mollusca
Protein Sequence Analysis
Sequence Analysis
Nucleotides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Nagle, G. T., Painter, S. D., Blankenship, J. E., Dixon, J. D., & Kurosky, A. (1986). Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia. Journal of Biological Chemistry, 261(17), 7853-7859.

Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia. / Nagle, G. T.; Painter, S. D.; Blankenship, J. E.; Dixon, J. D.; Kurosky, A.

In: Journal of Biological Chemistry, Vol. 261, No. 17, 1986, p. 7853-7859.

Research output: Contribution to journalArticle

Nagle, GT, Painter, SD, Blankenship, JE, Dixon, JD & Kurosky, A 1986, 'Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia', Journal of Biological Chemistry, vol. 261, no. 17, pp. 7853-7859.
Nagle, G. T. ; Painter, S. D. ; Blankenship, J. E. ; Dixon, J. D. ; Kurosky, A. / Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia. In: Journal of Biological Chemistry. 1986 ; Vol. 261, No. 17. pp. 7853-7859.
@article{24d03f1cd500455fbec0a647a51b3f35,
title = "Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia",
abstract = "Three peptide complexes which can induce egg laying in Aplysia were isolated from the atrial gland of the marine mollusc Aplysia californica and chemically characterized. Amino acid sequence analyses established the covalent structures, including disulfide assignments, of all three dimeric complexes. Each complex consisted of an identical 18-residue peptide (A-AP) which was disulfide-bonded to a 36-residue peptide that was homologous to bag cell egg-laying hormone (EHL). The primary structure of A-AP was determined to be: NH2-Asp-Ser-Asp-Val-Ser-Leu-Phe-Asn-Gly-Asp-Leu-Leu-Pro-Asn -Gly-Arg-Cys-Ser-COOH. The primary structure of one of the three ELH-regulated peptides (A-ELH) was determined to be NH2-Ile-Ser-Ile-Asn-Gln-Asp-Leu-Lys-Ala-Ile-Thr-Asp-Met-Leu -Leu-Thr-Glu-Gln-Ile-Gln-Ala-Arg-Arg-Arg-Cys-Leu-Asp-Ala-Leu -Arg-Gln-Arg-Leu-Leu-Asp-Leu-COOH. The two ELH-related peptides, [Ala27]A-ELH and [Gln23, Ala27]A-ELH, differed from A-ELH at 1 and 2 residues, respectively. Both [Ala27]A-ELH and [Gln23, Ala27]A-ELH were novel peptide sequences representing products of as yet uncharacterized genes within the ELH family. These structural studies provide the first direct chemical evidence that (a) an 18-residue peptide (A-AP) derived from a polypeptide precursor encoded by the A gene, as predicted from nucleotide sequence analysis, occurs in the atrial gland; (b) the Cys17 residue of A-AP is disulfide-bonded to Cys25 of A-ELH; and (c) A-AP also occurs disulfide-bonded to two additional, previously undescribed ELH-related peptides, [Ala27]A-ELH and [Gln23, Ala27]A-ELH.",
author = "Nagle, {G. T.} and Painter, {S. D.} and Blankenship, {J. E.} and Dixon, {J. D.} and A. Kurosky",
year = "1986",
language = "English (US)",
volume = "261",
pages = "7853--7859",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "17",

}

TY - JOUR

T1 - Evidence for the expression of three genes encoding homologous atrial gland peptides that cause egg laying in Aplysia

AU - Nagle, G. T.

AU - Painter, S. D.

AU - Blankenship, J. E.

AU - Dixon, J. D.

AU - Kurosky, A.

PY - 1986

Y1 - 1986

N2 - Three peptide complexes which can induce egg laying in Aplysia were isolated from the atrial gland of the marine mollusc Aplysia californica and chemically characterized. Amino acid sequence analyses established the covalent structures, including disulfide assignments, of all three dimeric complexes. Each complex consisted of an identical 18-residue peptide (A-AP) which was disulfide-bonded to a 36-residue peptide that was homologous to bag cell egg-laying hormone (EHL). The primary structure of A-AP was determined to be: NH2-Asp-Ser-Asp-Val-Ser-Leu-Phe-Asn-Gly-Asp-Leu-Leu-Pro-Asn -Gly-Arg-Cys-Ser-COOH. The primary structure of one of the three ELH-regulated peptides (A-ELH) was determined to be NH2-Ile-Ser-Ile-Asn-Gln-Asp-Leu-Lys-Ala-Ile-Thr-Asp-Met-Leu -Leu-Thr-Glu-Gln-Ile-Gln-Ala-Arg-Arg-Arg-Cys-Leu-Asp-Ala-Leu -Arg-Gln-Arg-Leu-Leu-Asp-Leu-COOH. The two ELH-related peptides, [Ala27]A-ELH and [Gln23, Ala27]A-ELH, differed from A-ELH at 1 and 2 residues, respectively. Both [Ala27]A-ELH and [Gln23, Ala27]A-ELH were novel peptide sequences representing products of as yet uncharacterized genes within the ELH family. These structural studies provide the first direct chemical evidence that (a) an 18-residue peptide (A-AP) derived from a polypeptide precursor encoded by the A gene, as predicted from nucleotide sequence analysis, occurs in the atrial gland; (b) the Cys17 residue of A-AP is disulfide-bonded to Cys25 of A-ELH; and (c) A-AP also occurs disulfide-bonded to two additional, previously undescribed ELH-related peptides, [Ala27]A-ELH and [Gln23, Ala27]A-ELH.

AB - Three peptide complexes which can induce egg laying in Aplysia were isolated from the atrial gland of the marine mollusc Aplysia californica and chemically characterized. Amino acid sequence analyses established the covalent structures, including disulfide assignments, of all three dimeric complexes. Each complex consisted of an identical 18-residue peptide (A-AP) which was disulfide-bonded to a 36-residue peptide that was homologous to bag cell egg-laying hormone (EHL). The primary structure of A-AP was determined to be: NH2-Asp-Ser-Asp-Val-Ser-Leu-Phe-Asn-Gly-Asp-Leu-Leu-Pro-Asn -Gly-Arg-Cys-Ser-COOH. The primary structure of one of the three ELH-regulated peptides (A-ELH) was determined to be NH2-Ile-Ser-Ile-Asn-Gln-Asp-Leu-Lys-Ala-Ile-Thr-Asp-Met-Leu -Leu-Thr-Glu-Gln-Ile-Gln-Ala-Arg-Arg-Arg-Cys-Leu-Asp-Ala-Leu -Arg-Gln-Arg-Leu-Leu-Asp-Leu-COOH. The two ELH-related peptides, [Ala27]A-ELH and [Gln23, Ala27]A-ELH, differed from A-ELH at 1 and 2 residues, respectively. Both [Ala27]A-ELH and [Gln23, Ala27]A-ELH were novel peptide sequences representing products of as yet uncharacterized genes within the ELH family. These structural studies provide the first direct chemical evidence that (a) an 18-residue peptide (A-AP) derived from a polypeptide precursor encoded by the A gene, as predicted from nucleotide sequence analysis, occurs in the atrial gland; (b) the Cys17 residue of A-AP is disulfide-bonded to Cys25 of A-ELH; and (c) A-AP also occurs disulfide-bonded to two additional, previously undescribed ELH-related peptides, [Ala27]A-ELH and [Gln23, Ala27]A-ELH.

UR - http://www.scopus.com/inward/record.url?scp=0023009062&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023009062&partnerID=8YFLogxK

M3 - Article

VL - 261

SP - 7853

EP - 7859

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 17

ER -