Identification of a functional cyclic adenosine 3',5'-monophosphate response element in the 5'-flanking region of the gene for transition protein 1 (TP1), a basic chromosomal protein of mammalian spermatids

• Published in: Biology of reproduction Vol. 51; no. 6; pp. 1322 - 1329
• Main Authors: Kistler, M K, Sassone-Corsi, P, Kistler, W S
• Format: Journal Article
• Language: English
• Published: Madison, WI Society for the Study of Reproduction 01.12.1994
• Subjects: Animals; Base Sequence; Biological and medical sciences; Cell Nucleus - chemistry; Choriocarcinoma; Chromosomal Proteins, Non-Histone - analysis; Chromosomal Proteins, Non-Histone - genetics; Chromosomal Proteins, Non-Histone - metabolism; Consensus Sequence; Conserved Sequence; Cyclic AMP Response Element Modulator; Cyclic AMP-Dependent Protein Kinases - biosynthesis; DNA - analysis; DNA - chemistry; DNA - genetics; DNA-Binding Proteins - genetics; DNA-Binding Proteins - immunology; DNA-Binding Proteins - metabolism; Enzyme Induction; Fundamental and applied biological sciences. Psychology; Gene Expression; Immune Sera - immunology; Male; Mammalia; Mammalian male genital system; Molecular Sequence Data; Morphology. Physiology; Nuclear Proteins - chemistry; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; Oligonucleotides - analysis; Oligonucleotides - chemistry; Oligonucleotides - genetics; Promoter Regions, Genetic; Rats; Rats, Sprague-Dawley; Repressor Proteins; Sequence Homology, Nucleic Acid; Testis - chemistry; Transfection; Tumor Cells, Cultured; Vertebrates: reproduction; Chromosome condensation; Vertebrata; Mammalia; Rat; Nucleotide sequence; Basic protein; Rodentia; Cyclic AMP; Response element; Nuclear protein; Spermatid; Transition protein 1
• DOI: 10.1095/biolreprod51.6.1322
• ISSN: 0006-3363

Transition protein 1 (TP1) is a small basic chromosomal protein that appears in mammalian spermatids during the period of chromatin condensation. The gene for TP1 from several species contains an apparent cAMP response element (CRE) in the immediate 5'-flanking region. The recent identification of high expression of the novel CRE-activating protein (CREM tau) in advanced testicular germ cells provided a stimulus to ask whether or not the TP1 CRE is functional. To this end we show both by gel retardation and by footprint assays that TP1 CRE forms specific bound complexes with proteins in whole testis nuclear extracts and that these complexes involve CREM as evidenced by recognition by a specific antibody. In addition, the TP1 CRE forms specific bound complexes with bacterially expressed CREM tau. Finally, the TPI CRE conveys protein kinase A-dependent induction to a linked chloramphenicol acetyl transferase gene when transfected into JEG-3 cells. Accordingly, TP1 is a good candidate for a testis-specific gene subject to CREM tau regulation.