Dataset Information


Structure-function relations in the NTPase domain of the antiviral tRNA ribotoxin Escherichia coli PrrC.

ABSTRACT: Breakage of tRNA by Escherichia coli anticodon nuclease PrrC (EcoPrrC) underlies a host antiviral response to phage T4 infection. Expression of EcoPrrC is cytocidal in yeast, signifying that PrrC ribotoxicity crosses phylogenetic domain boundaries. EcoPrrC consists of an N-terminal NTPase module that resembles ABC transporters and a C-terminal nuclease module that is sui generis. PrrC homologs are prevalent in many other bacteria. Here we report that Haemophilus influenzae PrrC is toxic in E. coli and yeast. To illuminate structure-activity relations, we conducted a new round of mutational analysis of EcoPrrC guided by primary structure conservation among toxic PrrC homologs. We indentify 17 candidate active site residues in the NTPase module that are essential for toxicity in yeast when EcoPrrC is expressed at high gene dosage. Their functions could be educed by integrating mutational data with the atomic structure of the transition-state complex of a homologous ABC protein.


PROVIDER: S-EPMC3312988 | BioStudies | 2012-01-01

REPOSITORIES: biostudies

Similar Datasets

2011-01-01 | S-EPMC3025547 | BioStudies
2008-01-01 | S-EPMC2610378 | BioStudies
2015-01-01 | S-EPMC4619093 | BioStudies
2020-01-01 | S-EPMC7049728 | BioStudies
2018-01-01 | S-EPMC6103680 | BioStudies
2014-01-01 | S-EPMC4070052 | BioStudies
1000-01-01 | S-EPMC3799443 | BioStudies
2001-01-01 | S-EPMC59754 | BioStudies
2010-01-01 | S-EPMC2978558 | BioStudies
1000-01-01 | S-EPMC3874168 | BioStudies