Jump to main content
Jump to site search

Issue 3, 2012
Previous Article Next Article

Modular recognition of nucleic acids by PUF, TALE and PPRproteins

Author affiliations

Abstract

Sequence specific binding of DNA and RNA is of fundamental importance in the regulation of cellular gene expression. Because of their modular structure repeat domain proteins are particularly well suited for these processes and have been widely adopted throughout evolution. Detailed biochemical and structural data has revealed the key residues responsible for recognition of RNA by Pumilio and FBF homology (PUF) repeat proteins and shown that the base specificity can be predicted and re-engineered. Recent work on the DNA-binding properties of transcription activator-like effector (TALE) proteins has shown that their specificity also relies on only a few key residues with a predictable code that can be used to design new DNA-binding proteins. Although less well understood, pentatricopeptide repeat (PPR) proteins contain motifs that appear to contribute to RNA recognition and comparisons to TALE and PUF proteins may help elucidate the code by which they recognize their RNA targets. Understanding how repeat proteins bind nucleic acids enables their biological roles to be uncovered and the design of engineered proteins with predictable RNA and DNA targets for use in biotechnology.

Graphical abstract: Modular recognition of nucleic acids by PUF, TALE and PPR proteins

Back to tab navigation

Article information


Submitted
24 Sep 2011
Accepted
07 Dec 2011
First published
10 Jan 2012

Mol. BioSyst., 2012,8, 699-708
Article type
Review Article

Modular recognition of nucleic acids by PUF, TALE and PPR proteins

A. Filipovska and O. Rackham, Mol. BioSyst., 2012, 8, 699
DOI: 10.1039/C2MB05392F

Search articles by author

Spotlight

Advertisements