Demonstration of the role of the DnaK chaperone system in assembly of 30S ribosomal subunits using a purified in vitro system.
Recently, there has been controversy regarding the ability of the DnaK chaperone system to facilitate Escherichia coli 30S subunit assembly at otherwise nonpermissive conditions. Here, we present additional data indicating that purified DnaK chaperone assembled 30S subunits are functional. Additionally, explanations for reported differences are discussed.
Maki
Jennifer A
JA
Iowa State University, Department of Biochemistry, Biophysics, and Molecular Biology, Ames, Iowa 50011, USA.
Southworth
Daniel R
DR
Culver
Gloria M
GM
D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology*; D066298:In Vitro Techniques; D018832:Molecular Chaperones / Q000502:physiology*; D012270:Ribosomes / Q000737:chemistry*
D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; C063842:dnaK protein, E coli