Rapid and Selective Cloning of Monitor Peptide, a Novel Cholecystokinin-releasing Peptide, Using Minimal Amino Acid Sequence and the Polymerase Chain Reaction

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Abstract
CDNA transcripts encoding rat monitor peptide (MP) have been cloned from a .lambda.-ZAP-II phage library using minimal specific amino acid sequence (six residues), the polymerase chain reaction (PCR), and multivalent PCR probes to distinguish MP transcripts from those that encode a closely related peptide, pancreatic secretory trypsin inhibitor. DNA sequence analysis of 3 cDNA transcripts, MP1-3, revealed the complete amino acid sequence of the prepeptide (79 residues) including an 18-residue hydrophobic signal sequence at the NH2 terminus. Sequence divergence in both coding and 3'' non-coding regions indicates a potential exon-exon junction with alternative splicing, which results in a truncated peptide with Arg 58 at the COOH terminus as well as alternative selection of poly(A) signals, respectively. The 5'' nontranslated region of MP1 mRNA (282 nucleotides (nt)) contains four upstream ATGs. Conserved structure between MP and anionic trypsinogen mRNAs within 9 nt immediately upstream of the AUG initiation codon may be involved in coupling the expression of MP with anionic trypsinogen, a condition which appears to be required to monitor the intake of dietary protein in the rat.

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