Primary structure of the precursor for the anthozoan neuropeptide Antho-RFamide from Renilla köllikeri: Evidence for unusual processing enzymes

TY - JOUR

T1 - Primary structure of the precursor for the anthozoan neuropeptide Antho-RFamide from Renilla köllikeri: Evidence for unusual processing enzymes

AU - Reinscheid, R K

AU - Grimmelikhuijzen, C J

PY - 1994/3/1

Y1 - 1994/3/1

N2 - Neuropeptides containing the C-terminal sequence Arg-Phe-NH2 are an important group of hormones mediating or modulating neuronal communication. Arg-Phe-NH2 peptides are abundant in evolutionarily "old" nervous systems such as those of coelenterates, the lowest animal group having a nervous system. Here, we have cloned the precursor protein for the anthozoan neuropeptide Antho-RFamide (<Glu-Gly-Arg-Phe-NH2) from the sea pansy Renilla köllikeri. This precursor contains 36 copies of immature Antho-RFamide (Gln-Gly-Arg-Phe-Gly) and two additional putative neuropeptide sequences, which are regularly distributed over the precursor protein. Of the 36 Antho-RFamide sequences, 29 copies are separated by the five amino acid spacer sequence Arg-Glu/Gly-Asn/Ser/Asp-Glu/Lys-Glu. This implicates processing at single Arg and single Glu residues. Endoproteolytic cleavage at the C-terminal side of paired or single basic residues is a well known initial step in the maturation of precursor proteins. Cleavage at the C-terminal side of acidic residues, however, is unusual and must be catalyzed by a new type of processing enzyme. This processing enzyme is most likely to be an endoprotease, because the simplest way to generate Antho-RFamide is by endoproteolytic cleavage at the C-terminal side of Glu residues. The enzyme could also be an aminopeptidase, but in this case other proteases must be involved. As a possible alternative, one single "unspecific" aminopeptidase could cleave at Glu, Asp, Gly, Asn, Ser, and possibly also at other residues, and thus liberate all Antho-RFamide sequences. The processing of one precursor molecule probably yields 38 neuropeptides.(ABSTRACT TRUNCATED AT 250 WORDS)

AB - Neuropeptides containing the C-terminal sequence Arg-Phe-NH2 are an important group of hormones mediating or modulating neuronal communication. Arg-Phe-NH2 peptides are abundant in evolutionarily "old" nervous systems such as those of coelenterates, the lowest animal group having a nervous system. Here, we have cloned the precursor protein for the anthozoan neuropeptide Antho-RFamide (<Glu-Gly-Arg-Phe-NH2) from the sea pansy Renilla köllikeri. This precursor contains 36 copies of immature Antho-RFamide (Gln-Gly-Arg-Phe-Gly) and two additional putative neuropeptide sequences, which are regularly distributed over the precursor protein. Of the 36 Antho-RFamide sequences, 29 copies are separated by the five amino acid spacer sequence Arg-Glu/Gly-Asn/Ser/Asp-Glu/Lys-Glu. This implicates processing at single Arg and single Glu residues. Endoproteolytic cleavage at the C-terminal side of paired or single basic residues is a well known initial step in the maturation of precursor proteins. Cleavage at the C-terminal side of acidic residues, however, is unusual and must be catalyzed by a new type of processing enzyme. This processing enzyme is most likely to be an endoprotease, because the simplest way to generate Antho-RFamide is by endoproteolytic cleavage at the C-terminal side of Glu residues. The enzyme could also be an aminopeptidase, but in this case other proteases must be involved. As a possible alternative, one single "unspecific" aminopeptidase could cleave at Glu, Asp, Gly, Asn, Ser, and possibly also at other residues, and thus liberate all Antho-RFamide sequences. The processing of one precursor molecule probably yields 38 neuropeptides.(ABSTRACT TRUNCATED AT 250 WORDS)

KW - Amino Acid Sequence

KW - Animals

KW - Base Sequence

KW - Cnidaria

KW - DNA, Complementary

KW - Molecular Probes

KW - Molecular Sequence Data

KW - Neuropeptides

KW - Protein Precursors

KW - Protein Processing, Post-Translational

KW - Pyrrolidonecarboxylic Acid

M3 - Journal article

C2 - 7906718

SN - 0022-3042

VL - 62

SP - 1214

EP - 1222

JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

IS - 3

ER -