BY RON MAGOLDA
Medical Products Department
E.I. Du Pont de Nemours & Co.
G-binding proteins have been implicated in a variety of biological processes. A structural analysis of this interesting class of proteins has been presented. P.Woolley, B.F.C. Clark, “Homologies in the structures of G-binding proteins: an analysis based on elongation factor EF-Tu,” BioTechnology, 7, 9 13-20, September 1989. (Aarhus University, Arhus, Denmark).
The biosynthesis of the antibiotic thiostrepton presented several structural and biochemical challenges, which this communication overcomes.
·P. Zhou, D. O’Hagan, U. Mocek, Z. Zeng, L.-D. Yuen, et al., “Biosynthesis of the antibiotic thiostrepton, methylation of tryptophan in the formation of the quinaldic acid moiety by transfer of the methionine methyl group with net retention of configuration,” Journal of the American Chemical Society, 111, 7274-6, 30 August 1989. (University of Washington, Seattle; Ohio State University, Columbus; Los Alamos National Laboratory, N.Mex.)
" Site-specific binding of reporter groups to duplex DNA has been the objective of several labs. Exploiting triple helix formation has been a very effective tactic in causing cooperative binding of oligonucleotides to duplex DNA.
S.A. Strobel, P.B. Dervan, “Cooperative site specific binding of oligonucleotides to duplex DNA,” Journal of the American Chemical Society, 111, 7286-7, 30 August 1989. (California Institute of Technology, Pasadena)
Structural examination of proteinases and proteinase inhibitors has sparked an evolutionary connection. This link offers an insight into the global understanding of protein and inhibitor interactions.
T.E. Creighton, N.J. Darby, “Functional evolutionary divergence of proteolytic enzymes and their inhibitors,” Trends in BiochemicalSciences, 14,319-24, August 1989. (MRC Laboratory of Molecular Biology, Cambridge, U.K.)
" Spirocarbocyclization is a synthetically challenging transformation. A novel method for the preparation of this class of compounds in moderate yields has been reported.
A.S. Kende, R.C. Newbold, “The vinylogous Conia rearrangement: a masked ene reaction,” Tetrahedron Letters, 30 (33), 4329-32, 1989. (University of Rochester, N.Y)
" The preparation of myo-inositol phosphate, the putative second messenger, has been the centerpiece of signal transduction studies. A recent work offers convenient routes to several of these interesting biomolecules.
D.C. Billington, R. Baker, J.J. Kulagowski, I.M. Mawer, “The total synthesis of myo-inositol phosphates via myo-inositol orthoformate,” Journal of the Chemical Society, Perkin Transactions 1, 8, 1423-9, August 1989. (Merck Sharp & Dohme Research Laboratories, Essex, U.K. & West Point, Pa.)
" Since the discovery of the “zinc fingers,” the biological role of this protein motif continues to expand. Two articles provide a three-dimensional structural view and a new biological utility for zinc fingers.
M.S. Lee, G.P. Gippert, K.V. Soman, D.A. Case, P.E. Wright, “Three-dimensional solution structure of a single zinc finger DNA-binding domain,” Science, 245, 635-7, 11 August 1989. (Research Institute of Scripps Clinic, La Jolla, Calif.)
T.B. Rajavashisth, A.K. Taylor, A. Andalibi, K.L. Svenson, A.J. Lusis, “Identification of a zinc finger protein that binds to the sterol regulatory element,” Science, 245, 640-3, 11 August 1989. (University of California, Los Angeles)
" Two new fungal-derived natural products that can block histamine-release from mast cells have been identified.
N. Kawahara, K. Nozawa, S. Nakajima, K. Kawai, M. Yamazaki, “Novel epitetrathiodioxopiperazines, emethalli- cins B and C, as potent inhibitors of compound 48/80-induced histamine release, from Emericella heterothallica,” Journal of the Chemical Society, Chemical Communications, 14, 951-2, 15 July 1989. (Hoshi University, Tokyo, Japan; Chiba University, Japan)
Mammastatin is a polypeptide secreted from normal human mammary cells. Investigators report that this endogenous peptide can inhibit the growth of transformed human mammary cell lines. The potential utility of mammastatin for the treatment of human breast cancer is also proposed.
P.R. Ervin, Jr., M.S. Kaminski, R.L. Cody, M.S. Wicha, “Production of mammastatin, a tissue-specific growth inhibitor, by normal human mammary cells,” Science, 244, 1585-7, 30 June 1989. (University of Michigan Cancer Center, Ann Arbor)