A tale of two polymers: new insights into helical filaments
- 1 August 2003
- journal article
- review article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 4 (8) , 621-631
- https://doi.org/10.1038/nrm1176
Abstract
Many proteins function as helical polymers within the cell. Two intensively studied examples are eukaryotic actin and bacterial RecA, which belong to two different protein superfamilies. However, most other members of these superfamilies do not polymerize into helical filaments. General features of polymorphism, cooperativity and allostery that emerge from studies of eukaryotic actin and bacterial RecA raise more general issues about how conserved these filamentous structures have been during evolution.Keywords
This publication has 104 references indexed in Scilit:
- Insights into DNA recombination from the structure of a RAD51–BRCA2 complexNature, 2002
- Crystal Structure of Arp2/3 ComplexScience, 2001
- Probing the structure of F-actin: cross-links constrain atomic models and modify actin dynamics 1 1Edited by M. F. MoodyJournal of Molecular Biology, 2001
- Does a Stretched DNA Structure Dictate the Helical Geometry of RecA-like Filaments?Journal of Molecular Biology, 2001
- An atomic model of crystalline actin tubes: combining electron microscopy with X-ray crystallographyJournal of Molecular Biology, 1998
- Crystal structure of a DExx box DNA helicaseNature, 1996
- Refinement of the F-Actin Model against X-ray Fiber Diffraction Data by the Use of a Directed Mutation AlgorithmJournal of Molecular Biology, 1993
- DNA Conformation Induced by the Bacteriophage T4 UvsX Protein Appears Identical to the Conformation Induced by the Escherichia coli RecA ProteinJournal of Molecular Biology, 1993
- The structure of the E. coli recA protein monomer and polymerNature, 1992
- Detection of conformational changes in actin by proteolytic digestion: Evidence for a new monomeric speciesJournal of Molecular Biology, 1976