E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides
| Autor: | Pradeep Parrack, Mathew Sajish, Debojyoti De, Dipak Dutta, Neha Dhimole, Balaji Prakash, Sushil Kumar Tomar, Nikhil Jain, Abu Rafay Khan |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
GTP'
Molecular Sequence Data Biophysics Ribosome biogenesis GTPase Ribosome Subunits Large Bacterial Biology Guanosine triphosphate Ribosome Biochemistry Article Ribosome assembly 03 medical and health sciences chemistry.chemical_compound GTP-binding protein regulators Adenosine Triphosphate GTP-Binding Proteins Escherichia coli ATPase Amino Acid Sequence Cloning Molecular Molecular Biology 030304 developmental biology 50S 0303 health sciences 030306 microbiology Nucleotides Escherichia coli Proteins Hydrolysis HflX Cell Biology 3. Good health chemistry rRNA binding protein Ribosome binding GTPase Guanosine Triphosphate |
| Zdroj: | Biochemical and Biophysical Research Communications |
| ISSN: | 1090-2104 0006-291X |
| Popis: | HflX is a GTP binding protein of unknown function. Based on the presence of the hflX gene in hflA operon, HflX was believed to be involved in the lytic-lysogenic decision during phage infection in Escherichia coli. We find that E. coli HflX binds 16S and 23S rRNA – the RNA components of 30S and 50S ribosomal subunits. Here, using purified ribosomal subunits, we show that HflX specifically interacts with the 50S. This finding is in line with the homology of HflX to GTPases involved in ribosome biogenesis. However, HflX-50S interaction is not limited to a specific nucleotide-bound state of the protein, and the presence of any of the nucleotides GTP/GDP/ATP/ADP is sufficient. In this respect, HflX is different from other GTPases. While E. coli HflX binds and hydrolyses both ATP and GTP, only the GTP hydrolysis activity is stimulated by 50S binding. This work uncovers interesting attributes of HflX in ribosome binding. |
| Databáze: | OpenAIRE |
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