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How the amino acid series of a protein determines its third-dimensional constitution is an enormous challenge in biology and chemistry. top specialists within the fields of NMR spectroscopy, X-ray crystallography, protein engineering and molecular modeling provide provocative insights into present perspectives at the protein folding challenge and diverse points for destiny growth.
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Additional info for Ciba Foundation Symposium 170 - Regulation of the Eukaryotic Cell Cycle
Cell 66:995-1013 Ogas J, Andrews BJ, Herskowitz I 1991 Transcriptional activation of CLNI, CLNZ, and a putative new G1 cyclin (HCS26) by SWI4, a positive regulator of G1-specific transcription. Cell 66: 1015-1026 Pringle JR, Hartwell J H 1981 The Saccharomyces cerevisiae life cycle. In: Strathern JN, Jones EW, Broach JR (eds) The molecular biology of the yeast Saccharomyces: life cycle & inheritance. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, p97-142 Richardson HE, Wittenberg C, Cross F, Reed SI 1989 An essential G1 function for cyclinlike proteins in yeast.
Although at present little is known about the partners of each of these new CdcZrelated proteins, or their activation profile in the cell cycle, it is plausible that in higher eukaryotes the existence of different cdc2 homologues puts the cell cycle machinery under very tight control by allowing separate transcriptional and post-transcriptional regulation at each transition point. 32 Marcote et al We became interested in the activation of the cyclin A-dependent kinase in the human cell cycle after finding that it is activated in interphase and that it can form complexes in vivo with the adenovirus E1A oncoprotein (Giordano et a1 1989, Pines & Hunter 1990), suggesting that an alteration of cyclin A function is involved in the process of cellular immortalization mediated by E l A.
Indeed, cyclin B is synthesized in late G1 and binds Cdc2, but the complex formed is rapidly inactivated by a Thr/Tyr kinase (probably the wee1 protein kinase and an additional kinase identified in S . pombe, mikl), which phosphorylates Cdc2 on TyrlS (and probably Thrl4) (for a review, see Fleig & Gould 1991). Both residues are located within a conserved motif present in all protein kinases and their phosphorylation in Cdc2 is thought to prevent ATP binding. Tyrosine dephosphorylationof Cdc2 is dependent upon completion of DNA replication; in the presence of unreplicated DNA the cyclin B-bound Cdc2 is phosphorylated on TyrlS and inactivated (Gould & Nurse 1989, Krek & Nigg 1991, Norbury et a1 1991).
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