Jump to main content
Jump to site search

Issue 12, 2017
Previous Article Next Article

Conformational heterogeneity in tails of DNA-binding proteins is augmented by proline containing repeats

Author affiliations

Abstract

A cationic terminal extension or tail is a common feature of many DNA-binding proteins. We show that a particular type of tail rich in proline, alanine and lysine belongs to the class of ‘flexible disorder’ and consists of characteristic pentapeptide repeats. Our designed peptides, (AAKKA)1–4 and (PAKKA)1–4, represent the tails of several bacterial DNA-binding proteins. Enhanced conformational sampling of these representative peptides using accelerated molecular dynamic simulations supported by circular dichroism spectroscopy and nuclear magnetic resonance studies demonstrates the role of frequent and interspersed prolines in augmenting conformational heterogeneity of the peptide backbone. Analysis of circular variance of backbone dihedral angles indicates alternating regions of relative rigidity and flexibility along the peptide sequence due to prolines. Preferred placement of lysines in the regions of higher backbone flexibility might improve DNA-binding by conformational selection. Our results could be relevant for rational de novo design of disordered peptides.

Graphical abstract: Conformational heterogeneity in tails of DNA-binding proteins is augmented by proline containing repeats

Back to tab navigation

Supplementary files

Publication details

The article was received on 08 Jul 2017, accepted on 25 Oct 2017 and first published on 26 Oct 2017


Article type: Paper
DOI: 10.1039/C7MB00412E
Citation: Mol. BioSyst., 2017,13, 2531-2544
  •   Request permissions

    Conformational heterogeneity in tails of DNA-binding proteins is augmented by proline containing repeats

    H. Khare, D. Dey, C. Madhu, D. Senapati, S. Raghothama, T. Govindaraju and S. Ramakumar, Mol. BioSyst., 2017, 13, 2531
    DOI: 10.1039/C7MB00412E

Search articles by author

Spotlight

Advertisements