Abstract

Experiments in the past year have succeeded in establishing the complete amino acid sequence of the lambda phage repressor and the nucleotide sequence of its corresponding gene as well as the nucleotide sequence of the cro gene. A repressor monomer is a protein containing two domains separated by a connector 42 amino acids long. The domains are separated by proteolytic cleavage, and each domain has been crystallized as has the cro protein. Recombinant DNA techniques have been used to produce special strains that make large amounts of these and other regulatory proteins. The structure and function of these molecules are currently under continuing investigation.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM022526-11
Application #
3563673
Study Section
(MG)
Project Start
1978-09-01
Project End
1987-11-30
Budget Start
1986-12-01
Budget End
1987-11-30
Support Year
11
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
Harvard University
Department
Type
DUNS #
071723621
City
Cambridge
State
MA
Country
United States
Zip Code
02138

  Publications

Sigal, G B; Bamdad, C; Barberis, A et al. (1996) A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance. Anal Chem 68:490-7
Astromoff, A; Ptashne, M (1995) A variant of lambda repressor with an altered pattern of cooperative binding to DNA sites. Proc Natl Acad Sci U S A 92:8110-4
Ohashi, Y; Brickman, J M; Furman, E et al. (1994) Modulating the potency of an activator in a yeast in vitro transcription system. Mol Cell Biol 14:2731-9
Reece, R J; Rickles, R J; Ptashne, M (1993) Overproduction and single-step purification of GAL4 fusion proteins from Escherichia coli. Gene 126:105-7
Bushman, F D; Shang, C; Ptashne, M (1989) A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressor. Cell 58:1163-71
Bushman, F D; Ptashne, M (1988) Turning lambda Cro into a transcriptional activator. Cell 54:191-7
Irwin, N; Ptashne, M (1987) Mutants of the catabolite activator protein of Escherichia coli that are specifically deficient in the gene-activation function. Proc Natl Acad Sci U S A 84:8315-9
Hochschild, A; Ptashne, M (1986) Cooperative binding of lambda repressors to sites separated by integral turns of the DNA helix. Cell 44:681-7
Hochschild, A; Ptashne, M (1986) Homologous interactions of lambda repressor and lambda Cro with the lambda operator. Cell 44:925-33
Ptashne, M (1986) Gene regulation by proteins acting nearby and at a distance. Nature 322:697-701

Showing the most recent 10 out of 17 publications