Vibrio cholerae YaeO is a Structural Homologue of RNA Chaperone Hfq that Inhibits Rho-dependent Transcription Termination by Dissociating its Hexameric State
| Autor: | Sriyans Jain, Kamalendu Pal, Malti Yadav, Ranjan Sen, Biplab Ghosh, Udayaditya Sen |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Protein Conformation Host Factor 1 Protein medicine.disease_cause 03 medical and health sciences Structure-Activity Relationship 0302 clinical medicine Bacterial Proteins Structural Biology Transcription (biology) medicine Amino Acid Sequence Molecular Biology Escherichia coli Vibrio cholerae Phylogeny 030304 developmental biology Hfq protein 0303 health sciences Binding Sites biology Chemistry RNA RNA-Binding Proteins Gene Expression Regulation Bacterial Sequence Analysis DNA RNA Helicase A Rho Factor Cell biology Docking (molecular) Antitermination Transcription Termination Genetic biology.protein Protein Multimerization 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Journal of molecular biology. 431(24) |
| ISSN: | 1089-8638 |
| Popis: | Rho-dependent transcription termination is a well-conserved process in bacteria. The Psu and YaeO proteins are the two established inhibitors of the ATP-dependent RNA helicase Rho protein of Escherichia coli. Here, we show a detailed sequence and phylogenetic analysis demonstrating that Vibrio cholerae YaeO (VcYaeO) is significantly distinct from its E. coli counterpart. VcYaeO induces significant growth defect on in vivo expression and inhibits in vitro functions of the V. cholerae Rho on directly binding to the latter. Through various biophysical techniques, we showed that interaction of VcYaeO disrupts the oligomeric state of the VcRho. Structure of VcYaeO solved at 1.75 A resolution, the first crystal structure of a YaeO protein, demonstrates a beta-sandwich fold distinct from the NMR structure of the EcYaeO. Interestingly, VcYaeO structurally resembles the Hfq protein, and like the latter, it exhibits ssDNA/RNA-binding properties. Docking studies demonstrate probable interactions of VcYaeO with VcRho and mode of inhibition of RNA binding to Rho. We propose that VcYaeO inhibits the function of the Rho protein via disruption of the latter's hexameric assembly and also likely by sequestering the RNA from the Rho primarybinding sites. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect