By J. L. Bos, B. M. T. Burgering, G. J. Pronk, A. M. M. de Vries-Smits, J. P. Medema (auth.), Prof. Dr. S. Papa, Prof. Dr. J. M. Tager (eds.)
This booklet includes a chain of experiences on chosen themes in the quickly and enormously increasing box of membrane biology. Its target is to focus on the main major and critical advances which were made in recent times in knowing the constitution, dynamics and features of cellphone membranes. parts coated during this monograph comprise: • sign Transduction • Membrane site visitors: Protein and Lipids • Bioenergetics: strength move and Membrane delivery • mobile Ion Homeostasis • development components and Adhesion Molecules • Structural research of Membrane Proteins • Membranes and illness. Biochemistry of phone Membranes may still function a benchmark for indicating crucial traces for destiny study in those components.
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Physiol. 25: CI85-CI88. Biochemistry of Cell Membranes ed. by S. Papa" J. M. Tager © 1995 Birkhauser Verlag Basel/Switzerland RAS proteins and control of the cell cycle in Saccharomyces cerevisiae O. Fasanot Dipartimento di Biologia Cellulare e della Sviluppo, Universita di Palermo, via Archiraff 22, 1-90123 Palermo, Italy The RASI and RAS2 genes of Saccharomyces cerevisiae Genes related to the mammalian H-, K-, and N-ras oncogenes were identified in S. cerevisiae by DNA hybridization techniques (for reviews, see Tamanoi, 1988; Gibbs and Marshall, 1989; Broach and Deschenes, 1990).
Res. Commum. 195: 484-489. Kolman, J. R. and Miller, G. (1993) Serine-173 of the EpsteinBarr virus ZEBRA protein is required for DNA binding and is target for casein kinase II phosphorylation. Proc. Natl. Acad. Sci. USA 90: 10115-10119. , Maridor, G. A. (1992) Casein kinase II is a predominantly nuclear enzyme. J. Cell Bioi. 116: 43-55. Q. P. F. (1990) Cyclic-AMP responsive transcriptional activation of CREB-327 involves interdependent phosphorylated subdomains. EMBO J. 9: 4455-4465. Li, H. J. (1992) Casein kinase II protein kinase is bound to lamina-matrix and phosphorylates lamin-like protein in isolated pea nuclei.
According to the rules of yeast genetics (dominant genes are indicated by three capital letters followed by a number), the yeast genes were denominated RAS 1 and RAS2 (collectively referred to as RAS). The corresponding RAS 1 and RAS2 proteins were 309 and 322 amino acids long, respectively. The sequence similarity between the human and yeast proteins was very high, reaching 90% identity at the level of the N-terminal 80 amino acids. As a consequence, perfect sequence conservation was observed at the level of those amino acids that are critical for the oncogenic activation of mammalian RAS proteins (12, 13, 61, human coordinates).