sup 31 P NMR spectra of an oligodeoxyribonucleotide duplex lac operator-repressor headpiece complex

Journal Article · Tue Jul 17 00:00:00 EDT 1990 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00480a005· OSTI ID:6290646

Karslake, C; Schroeder, S; Wang, Pei Ling; Gorenstein, D G ^[1]

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1. Purdue Univ., West Lafayette, IN (USA)

The interaction of a symmetric lac operator duplex, d(TGTGAGCGCTCACA){sub 2}, with the N-terminal 56-residue headpiece fragment of the lac repressor protein was monitored by {sup 31}P NMR spectroscopy. The changes in the {sup 31}P chemical shifts upon addition of the headpiece demonstrated an end point of two headpiece fragments per symmetric 14-mer duplex with each headpiece binding to the T1pG2pT3pG4pA5 ends of the duplex. The specific phosphate {sup 31}P perturbations observed are consistent with those residues implicated in protein binding by previous NMR, molecular biological, and biochemical techniques. Upon complexation, the {sup 31}P signals of phosphates G2-A5 showed upfield or downfield shifts (<0.2 ppm) while most other residues were unperturbed. The interactions were dependent on ionic strength. The {sup 31}P NMR data provide direct evidence for predominant recognition of the 5{prime} strand of the 5{prime}-TGTGA/3{prime}-ACACT binding site.

• OSTI ID: 6290646
• Journal Information: Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:28; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
BACTERIA
CELL CONSTITUENTS
CHEMICAL SHIFT
ESCHERICHIA COLI
GENE OPERONS
GENE REPRESSORS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MICROORGANISMS
MOLECULAR STRUCTURE
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEI
NUCLEIC ACIDS
NUCLEOPROTEINS
ODD-EVEN NUCLEI
OLIGONUCLEOTIDES
ORGANIC COMPOUNDS
PHOSPHORUS 31
PHOSPHORUS ISOTOPES
PLASMIDS
PROTEINS
RESONANCE
SPECTRA
STABLE ISOTOPES