Beushausen S, Lee E, Walker B, Bayley H
Laboratory of Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1641-5. doi: 10.1073/pnas.89.5.1641.
Previously, two forms of cAMP-dependent protein kinase catalytic subunit generated by mutually exclusive use of two internal exon cassettes (A1 and A2) were demonstrated in Aplysia neurons. Here, it is shown that there also exist catalytic subunits with alternative N termini derived from two exons, N1 and N2, expressed in combination with either of the internal cassettes. Processed transcripts including N1 or N2 sequences are of about equal abundance in the nervous system, arise through alternative promoter use, and encode catalytically active polypeptides. The N2 amino acid sequence is 21 residues longer than the N1 sequence and is homologous to the nonmyristoylated N terminus of the TPK1 gene product, a yeast catalytic subunit homolog. These data support the view that cAMP-dependent protein kinase activity in Aplysia neurons is produced by a complex array of regulatory and catalytic subunits that generate multiple holoenzymes with a spectrum of properties.
先前已证实在海兔神经元中存在两种形式的依赖环磷酸腺苷(cAMP)的蛋白激酶催化亚基,它们通过相互排斥地使用两个内部外显子盒(A1和A2)产生。在此表明,还存在具有源自两个外显子N1和N2的可变N末端的催化亚基,它们与任一内部盒组合表达。包含N1或N2序列的加工转录本在神经系统中的丰度大致相等,通过使用替代启动子产生,并编码具有催化活性的多肽。N2氨基酸序列比N1序列长21个残基,并且与酵母催化亚基同源物TPK1基因产物的非肉豆蔻酰化N末端同源。这些数据支持这样的观点,即海兔神经元中依赖cAMP的蛋白激酶活性是由一系列复杂的调节和催化亚基产生的,这些亚基产生具有一系列特性的多种全酶。