Heilmeyer L M, Serwe M, Weber C, Metzger J, Hoffmann-Posorske E, Meyer H E
Abteilung für Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, Federal Republic of Germany.
Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9554-8. doi: 10.1073/pnas.89.20.9554.
The primary structure of the alpha and beta subunits of phosphorylase kinase reveals that both proteins contain a carboxyl-terminal CA1A2X motif (where C is cysteine, A1 and A2 are aliphatic amino acids, and X is an uncharged amino acid), the recognition signal for a protein polyisoprenyltransferase. The product, a polyisoprenylated cysteine, can be detected by phenylthiocarbamoylamino acid analysis and by microsequencing following conversion to S-ethylcysteine. Mass spectrometry confirms a covalently linked farnesyl residue in both subunits. Tandem mass spectrometry localizes these modifications at the cysteine residues present in the carboxyl-terminal CAMQ and CLVS sequences of the alpha and beta subunits, respectively. Membrane association of phosphorylase kinase, probably mediated by these farnesyl residues, is discussed.
磷酸化酶激酶α和β亚基的一级结构显示，这两种蛋白质都含有一个羧基末端CA1A2X基序（其中C是半胱氨酸，A1和A2是脂肪族氨基酸，X是不带电荷的氨基酸），这是一种蛋白质多异戊二烯基转移酶的识别信号。该产物，即多异戊二烯化的半胱氨酸，可以通过苯硫代氨基甲酰氨基酸分析以及在转化为S-乙基半胱氨酸后进行微量测序来检测。质谱分析证实两个亚基中均存在共价连接的法尼基残基。串联质谱分析分别将这些修饰定位在α和β亚基羧基末端CAMQ和CLVS序列中的半胱氨酸残基上。文中讨论了可能由这些法尼基残基介导的磷酸化酶激酶与膜的结合。
