Role of the Rubisco small subunit. Final report for period May 1, 1997--April 30,2000 [electronic resource]

Ribulose Diphosphate Carboxylase; Chlamydomonas; Molecular Structure; Structure-activity Relationships; Catalysis; Progress Report; Mutagenesis; Dna Sequencing; Chloroplasts; Oxygenases.

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Bibliographic Details
Online Access: Online Access
Corporate Authors: University of Nebraska--Lincoln (Researcher), United States. Department of Energy. Chicago Operations Office (Researcher)
Format: Government Document Electronic eBook
Language:English
Published: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Energy Research ; distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2000.
Subjects:

MARC

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245 0 0 |a Role of the Rubisco small subunit. Final report for period May 1, 1997--April 30,2000  |h [electronic resource] 
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500 |a Spreitzer, Robert J. 
513 |a Final;  |b 05/01/1997 - 04/30/2000. 
520 3 |a CO₂ and O₂ are mutually competitive at the active site of ribulose-1,5-biphosphate (RuBP) carboxylase/oxygenase (Rubisco). Rubisco contains two subunits, each present in eight copies. The 15-kD small subunit is coded by a family of nuclear RbcS genes. Until now, the role of the small subunit in Rubisco structure or catalytic efficiency is not known. Because of other work in eliminating the two RbcS genes in the green algo Chlamydomonas reinhardtii, it is now possible to address questions about the structure-function relationships of the eukaryotic small subunit. There are three specific aims in this project: (1) Alanine scanning mutagenesis is being used to dissect the importance of the βA/βB loop, a feature unique to the eukaryotic small subunit. (2) Random mutagenesis is being used to identify additional residues or regions of the small subunit that are important for holoenzyme assembly and function. (3) Attempts are being made to express foreign small subunits in Chlamydomonas to examine the contribution of small subunits to holoenzyme assembly, catalytic efficiency, and CO₂/O₂ specificity. 
520 0 |a Ribulose Diphosphate Carboxylase; Chlamydomonas; Molecular Structure; Structure-activity Relationships; Catalysis; Progress Report; Mutagenesis; Dna Sequencing; Chloroplasts; Oxygenases. 
536 |b FG02-97ER20261. 
650 7 |a Ribulose Diphosphate Carboxylase.  |2 local. 
650 7 |a Chlamydomonas.  |2 local. 
650 7 |a Molecular Structure.  |2 local. 
650 7 |a Structure-activity Relationships.  |2 local. 
650 7 |a Catalysis.  |2 local. 
650 7 |a Progress Report.  |2 local. 
650 7 |a Mutagenesis.  |2 local. 
650 7 |a Dna Sequencing.  |2 local. 
650 7 |a Chloroplasts.  |2 local. 
650 7 |a Oxygenases.  |2 local. 
650 7 |a Basic Biological Sciences.  |2 edbsc. 
710 2 |a University of Nebraska--Lincoln.  |4 res. 
710 1 |a United States.  |b Department of Energy.  |b Office of Energy Research.  |4 spn. 
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710 1 |a United States.  |b Department of Energy.  |b Office of Scientific and Technical Information.  |4 dst. 
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