Gene Expression in Rhodopseudomonas Sphaeroides (Photosynthesis, Carboxylase, Membrane Biosynthesis
type: CreativeWork
description: A DNA-directed coupled transcription-translation system has been developed in cell-free extracts from the facultative phototroph, Rhodopseudomonas sphaeroides. The in vitro protein synthesizing system was active when prepared from either aerobically or anaerobically grown cells. Optimal activity was dependent upon use of extracts prepared freshly from early exponential phase cells, the method of cell breakage, and the length of preincubation of the extract (S-30), as well as the concentrations of S-30, DNA template, and cations. The cell-free system was used to study the physical and biochemical characterization of an enzymatically active form II ribulose-1,5-bisphosphate carboxylase which was synthesized and assembled in vitro from cloned R. sphaeroides DNA. The predominant enzymatically active oligomeric form of the in vitro synthesized and assembled RuBP carboxylase was a tetramer-hexamer, and assembly of the monomeric subunits to form active enzyme was dependent on the presence of a minimum number of subunits.
abstract: A DNA-directed coupled transcription-translation system has been developed in cell-free extracts from the facultative phototroph, Rhodopseudomonas sphaeroides. The in vitro protein synthesizing system was active when prepared from either aerobically or anaerobically grown cells. Optimal activity was dependent upon use of extracts prepared freshly from early exponential phase cells, the method of cell breakage, and the length of preincubation of the extract (S-30), as well as the concentrations of S-30, DNA template, and cations. The cell-free system was used to study the physical and biochemical characterization of an enzymatically active form II ribulose-1,5-bisphosphate carboxylase which was synthesized and assembled in vitro from cloned R. sphaeroides DNA. The predominant enzymatically active oligomeric form of the in vitro synthesized and assembled RuBP carboxylase was a tetramer-hexamer, and assembly of the monomeric subunits to form active enzyme was dependent on the presence of a minimum number of subunits.
author: Chory, Joanne
keywords: Biology, Microbiology
date published: 2014-12-16T06:12:51Z
date modified: 2026-07-22T22:26:04Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/71166