Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring.

ABSTRACT:

Background

The exosome complex is an essential RNA 3'-end processing and degradation machinery. In archaeal organisms, the exosome consists of a catalytic ring and an RNA-binding ring, both of which were previously reported to assume three-fold symmetry.

Methodology/principal findings

Here we report an asymmetric 2.9 A Sulfolobus solfataricus archaeal exosome structure in which the three-fold symmetry is broken due to combined rigid body and thermal motions mainly within the RNA-binding ring. Since increased conformational flexibility was also observed in the RNA-binding ring of the related bacterial PNPase, we speculate that this may reflect an evolutionarily conserved mechanism to accommodate diverse RNA substrates for degradation.

Conclusion/significance

This study

SUBMITTER: Lu C 

PROVIDER: S-EPMC2806925 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature