Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype. Journal Article uri icon

Overview

abstract

  • 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.

publication date

  • January 1, 2008

Date in CU Experts

  • March 13, 2015 12:56 PM

Full Author List

  • Elles LM; Uhlenbeck OC

author count

  • 2

citation count

  • 21

Other Profiles

International Standard Serial Number (ISSN)

  • 0305-1048

Electronic International Standard Serial Number (EISSN)

  • 1362-4962

Additional Document Info

start page

  • 41

end page

  • 50

volume

  • 36

issue

  • 1