Chemical modification of arginine residues in the lactose repressor
The lactose repressor protein was chemically modified with 2,3-butanedione and phenylglyoxal. Arginine reaction was quantitated by either amino aced analysis or incorporation of /sup 14/C-labeled phenylglyoxal. Inducer binding activity was unaffected by the modification of arginine residues, while both operator and nonspecific DNA binding activities were diminished, although to differing degrees. The correlation of the decrease in DNA binding activities with the modification of approx. 1-2 equiv of arginine per monomer suggests increased reactivity of a functionally essential residue(s). For both reagents, operator DNA binding activity was protected by the presence of calf thymus DNA, and the extent of reaction with phenylglyoxal was simultaneously diminished. This protection presumably results from steric restriction of reagent access to an arginine(s) that is (are) essential for DNA binding interactions. These experiments suggest that there is (are) an essential reactive arginine(s) critical for repressor binding to DNA.
- Research Organization:
- Rice Univ., Houston, TX
- OSTI ID:
- 5640147
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:20; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550601 -- Medicine-- Unsealed Radionuclides in Diagnostics
59 BASIC BIOLOGICAL SCIENCES
62 RADIOLOGY AND NUCLEAR MEDICINE
ALDEHYDES
AMINO ACIDS
ARGININE
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBOHYDRATES
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
DAYS LIVING RADIOISOTOPES
DISACCHARIDES
DNA
ELECTROPHORESIS
GENE REPRESSORS
GLYOXAL
ISOTOPES
LABELLED COMPOUNDS
LACTOSE
LIGHT NUCLEI
NUCLEI
NUCLEIC ACIDS
NUCLEOPROTEINS
ODD-ODD NUCLEI
OLIGOSACCHARIDES
ORGANIC ACIDS
ORGANIC COMPOUNDS
PH VALUE
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PROTEINS
PURIFICATION
RADIOASSAY
RADIOISOTOPES
SACCHARIDES
TRITIUM COMPOUNDS
UPTAKE