lac repressor changes conformation upon binding to poly[dA-T)] | Zendy

D E Kelsey | Zendy; Taylor Rounds | Zendy; Sheldon S. York | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

lac repressor changes conformation upon binding to poly[dA-T)]

Author(s) -

D E Kelsey,

Taylor Rounds,

Sheldon S. York

Publication year - 1979

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.76.6.2649

Subject(s) - repressor , tetramer , chemistry , dna , lac repressor , escherichia coli , fluorescence , stereochemistry , biochemistry , gene , gene expression , physics , quantum mechanics , enzyme

N-(Iodoacetylaminoethyl)-1-naphthylamine-5-sulfonate reacts with Escherichia coli lac repressor to selectively label cysteine-140 with the fluorescent N-(acetylaminoethyl)-1-naphthylamine-5-sulfonate group. The fluorescence intensity of this label decreases by 20% when labeled repressor associates with poly[d(A-T)]. Fifteen base pairs of poly[d(A-T)] per repressor tetramer are required to complete this decrease. Stopped-flow experiments have shown that the repressor undergoes at least two conformational changes as it binds to poly[d(A-T)], with half-lives of 5.0 +/- 1.2 msec and 3.5 +/- 1.0 sex. Quite likely, these conformational changes serve to strengthen the interaction of repressor with DNA.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research