Abstract
Synthetic 32P-labeled oligonucleotides have been used to identify the prostatic proline-rich polypeptide (PRP) mRNA which has partially been characterized. The 14-mer d(G-G-T-T-C-T-G-C-A-T-A-A-T-G) complementary to the coding sequence for His-Tyr-Ala-Glu-Pro, a sequence element occurring in all 38-residue PRP variants, hybridizes specifically with a 12.5-kilobase mRNA which is clearly androgen-controlled. This oligonucleotide was used as an efficient primer for the construction of a PRP-specific lambda gt10 cDNA library. The nucleotide sequence of the inserts from several recombinant clones has been determined. This structural analysis revealed a PRP mRNA encoding a large precursor containing a number of tandemly repeated units. Each repeat codes for a sequence of 100 amino acids in which the highly conserved PRP sequence is embedded. From this polyprotein the large number of PRP variants must be generated by a post-translational processing mechanism which is still unknown. The high degree of conservation of both nucleotide and amino acid sequence in the entire unit also indicates that the PRP gene(s) likely evolved by multiplication of a 300-base pair ancestral DNA sequence. This has resulted in a noninterrupted repetitive DNA coding segment which is detected at the genomic level.
Highlights
A Single 12.5-Kilobase Androgen-regulated mRNA Encoding Multiple Proline-rich Polypeptides in the Ventral Prostate of the Rat*
The nucleotide sequence of the inserts from several recombinant clones has been determined. This structural analysis revealed a PRP mRNA encoding a large precursor containing a number of tandemly repeated units
Each repeat codes for a sequence of 100 amino acids in which the highly conserved PRP seanalysis of these peptides has demonstrated that they constitute a heterogeneous group of small 38-residue-longpolypeptides with high sequence similarity which can be subdivided into five classes [6], based on amino acid substitutions at positions 6, 10, and 11 [7]
Summary
This oligonucleotide was used as an efficient primer for the construction of a PRP-specific XgtlO cDNA library. The nucleotide sequence of the inserts from several recombinant clones has been determined This structural analysis revealed a PRP mRNA encoding a large precursor containing a number of tandemly repeated units. In order to get some insight into the underlying molecular mechanisms responsible for this large complexity and to understand the processes whereby these small peptides are quence is embedded. From this polyprotein the large generated from a much larger precursor, we started a search number of PRP variantsmust be generated by a post- for the PRP-coding mRNA(s). This has resulted in a noninterrupted repetitive DNA coding segment which is detected at the genomic level
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