# REPRESSOR AND ANTIREPRESSOR PROTEINS OF BACTERIOPHAGE

> **NIH NIH R01** · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · 1992 · $322,131

## Abstract

The objective is to understand how proteins recognize specific
sequences of double stranded DNA and to understand how the
activities of gene regulatory proteins are controlled by
interactions with other proteins.  Genetic, biochemical, and
structural studies will be used to elucidate the detailed
mechanism by which the Arc and Mnt repressors of bacteriophage
P22 bind to their respective operator sequences, and to
characterize mutations that enhance or alter the binding
specificity of the lambda repressor and lambda Cro proteins.
Mutations that abolish or enhance cooperative interactions
between lambda repressor molecules bound at adjacent operator
sites will also be isolated, and the effects of these mutations on
protein-mediated DNA looping and the linear polymerization of
repressor in solution will be determined.  Finally, the mechanisms
of RecA-mediated and P22 antirepressor-mediated inactivation of
lambda repressor will be explored by studying the biochemical
properties of mutant proteins that display altered properties in
the inactivation reactions.

## Key facts

- **NIH application ID:** 3126892
- **Project number:** 5R01AI016892-13
- **Recipient organization:** MASSACHUSETTS INSTITUTE OF TECHNOLOGY
- **SAM.gov UEI:** E2NYLCDML6V1
- **Principal Investigator:** Robert T Sauer
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1992
- **Award amount:** $322,131
- **Award type:** 5
- **Project period:** 1980-04-01 → 1993-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3126892

## Citation

> US National Institutes of Health, RePORTER application 3126892, REPRESSOR AND ANTIREPRESSOR PROTEINS OF BACTERIOPHAGE (5R01AI016892-13). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3126892. Licensed CC0.

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