Abstract

One of the most central and discriminating processes in all living cells is achieved by specific interaction between DNA and protein. Many cellular regulations depend upon the accuracy of such specific interactions. However at present we know very little about the detailed mechanism of such interactions at atomic or structural level. None of the following questions are answered: Is there conformational change in protein and/or DNA when it recognizes specific sequence of DNA? How does this enzyme discriminate a specific sequence against a similar DNA sequence? Is there a third element, such as water molecules or metal ions, anions, etc., that participates in the specific recognition process? One of the simplest systems in which specific interactions between DNA and protein can be studied is the DNA restriction and modification system. The overall objective of this proposal is to determine 3-dimensional structures Of EcoRI restriction endonuclease and methylase, as well as their complexes with DNA of particular sequence by X-ray diffraction methods. The comparison between the 3-dimensional structures of enzymes alone and the complex between enzymes and DNA is likely to provide the answers to the questions above.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM029287-05
Application #
3276844
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1981-08-01
Project End
1986-11-30
Budget Start
1985-08-01
Budget End
1986-11-30
Support Year
5
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of California Berkeley
Department
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704

  Publications

Glaeser, R M; Tong, L; Kim, S H (1989) Three-dimensional reconstructions from incomplete data: interpretability of density maps at ""atomic"" resolution. Ultramicroscopy 27:307-18
Pearlman, D A; Kim, S H (1988) Conformational studies of nucleic acids. V. Sequence specificities in the conformational energetics of oligonucleotides: the homo-tetramers. Biopolymers 27:59-77
de Vos, A M; Tong, L; Milburn, M V et al. (1988) Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21. Science 239:888-93
Jancarik, J; de Vos, A; Kim, S H et al. (1988) Crystallization of human c-H-ras oncogene products. J Mol Biol 200:205-7
Kim, S H; de Vos, A M; Tong, L et al. (1988) ras oncogene proteins: three-dimensional structures, functional implications, and a model for signal transducer. Cold Spring Harb Symp Quant Biol 53 Pt 1:273-81
Kim, S H; Cech, T R (1987) Three-dimensional model of the active site of the self-splicing rRNA precursor of Tetrahymena. Proc Natl Acad Sci U S A 84:8788-92
Pearlman, D A; Kim, S H (1986) Conformational studies of nucleic acids: III. Empirical multiple correlation functions for nucleic acid torsion angles. J Biomol Struct Dyn 4:49-67
Pearlman, D A; Kim, S H (1986) Conformational studies of nucleic acids: IV. The conformational energetics of oligonucleotides: d(ApApApA) and ApApApA. J Biomol Struct Dyn 4:69-98
Holbrook, S R; Wang, A H; Rich, A et al. (1986) Local mobility of nucleic acids as determined from crystallographic data. II. Z-form DNA. J Mol Biol 187:429-40
Kim, S H; Pearlman, D A; Holbrook, S R et al. (1985) Structures of DNA containing psoralen crosslink and thymine dimer. Prog Clin Biol Res 172A:143-52

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