Journal
NUCLEIC ACIDS RESEARCH
Volume 36, Issue 1, Pages 41-50Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkm926
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Funding
- NATIONAL CENTER FOR RESEARCH RESOURCES [C06RR018850] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM060268] Funding Source: NIH RePORTER
- NCRR NIH HHS [C06 RR018850, 1C06RR018850-01] Funding Source: Medline
- NIGMS NIH HHS [R01-GM60268-08, R01 GM060268, R01-GM60268] Funding Source: Medline
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Escherichia coli DEAD-box protein A (DbpA) is an ATP-dependent RNA helicase with specificity for 23S ribosomal RNA. Although DbpA has been extensively characterized biochemically, its biological function remains unknown. Previous work has shown that a DbpA deletion strain is viable with little or no effect on growth rate. In attempt to elucidate a phenotype for DbpA, point mutations were made at eleven conserved residues in the ATPase active site, which have exhibited dominant-negative phenotypes in other DExD/H proteins. Biochemical analysis of these DbpA mutants shows the expected decrease in RNA-dependent ATPase activity and helix unwinding activity. Only the least biochemically active mutation, R331A, produces small colony phenotype and a reduced growth rate. This dominant slow growth mutant will be valuable to determine the cellular function of DbpA.
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