Abstract

1. DNA-Protein Interaction The first aim is to better understand the molecular basis of DNA-protein recognition and the regulation of gene expression. Studies will be continued of the cro repressor protein from bacteriophage lambda, for which the three-dimensional structure has been determined. Mutant cro proteins with unexpected changes in DNA binding and/or protein stabilities will also be studied crystallographically. Attempts will be continued to determine the structure of cro complexed with appropriate DNA fragments. Attempts to determine the structures of the MerR metalloregulatory protein and other DNA binding proteins, as well as complexes of these proteins with DNA will also be pursued. 2. Protein Folding, Function, and Evolution The second goal is to better understand the factors that determine the structure, stability, dynamics, folding and activity of proteins. Ongoing genetic, structural and thermodynamic studies of mutant phage lysozymes, as well as comparative studies of goose lysozyme, phage P22 lysozyme, and other proteins, provide a very favorable experimental framework within which to address these problem areas.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
2R37GM020066-17
Application #
3484331
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1979-01-01
Project End
1993-12-31
Budget Start
1989-01-01
Budget End
1989-12-31
Support Year
17
Fiscal Year
1989
Total Cost
Indirect Cost

  Institution

Name
University of Oregon
Department
Type
Organized Research Units
DUNS #
948117312
City
Eugene
State
OR
Country
United States
Zip Code
97403

  Publications

Juers, Douglas H; Rob, Beatrice; Dugdale, Megan L et al. (2009) Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli). Protein Sci 18:1281-92
Busam, Robert D (2008) Structure of Escherichia coli exonuclease I in complex with thymidine 5'-monophosphate. Acta Crystallogr D Biol Crystallogr 64:206-10
Juers, Douglas H; Lovelace, Jeffrey; Bellamy, Henry D et al. (2007) Changes to crystals of Escherichia coli beta-galactosidase during room-temperature/low-temperature cycling and their relation to cryo-annealing. Acta Crystallogr D Biol Crystallogr 63:1139-53
Tronrud, Dale E (2007) Introduction to macromolecular refinement. Methods Mol Biol 364:231-54
Wood, Zachary A; Weaver, Larry H; Brown, Patrick H et al. (2006) Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. J Mol Biol 357:509-23
Addlagatta, Anthony; Quillin, Michael L; Omotoso, Omonike et al. (2005) Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome. Biochemistry 44:7166-74
Ostheimer, Gerard J; Hadjivassiliou, Haralambos; Hadjivasiliou, Haralambos et al. (2005) Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces. J Mol Biol 345:51-68
Juers, Douglas H; Kim, Jaeseung; Matthews, Brian W et al. (2005) Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin. Biochemistry 44:16524-8
Yousef, Mohammad S; Matthews, Brian W (2005) Structural basis of Prospero-DNA interaction: implications for transcription regulation in developing cells. Structure 13:601-7
Addlagatta, Anthony; Hu, Xiaoyi; Liu, Jun O et al. (2005) Structural basis for the functional differences between type I and type II human methionine aminopeptidases. Biochemistry 44:14741-9

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