National Technical Reports Library

The National Technical Information Service acquires, indexes, abstracts, and archives the largest collection of U.S. government-sponsored technical reports in existence. The NTRL offers online, free and open access to these authenticated government technical reports. Technical reports and documents in its repository may be available online for free either from the issuing federal agency, the U.S. Government Publishing Office’s Federal Digital System website, or through search engines.

Details

Novel, Photosynthesis-Associated Thioredoxin-Like Gene.

DE2006850272

Publication Date	2006
Page Count	8
Abstract	We validated much of the previous work on TxlA in PCC 7942, although we have raised doubts about whether the original TxlXg phenotype was actually a homogeneous mutant. We showed that the TxlA homologue in PCC 6803, Sll1980, is required for both photoautotropic and heterotrophic growth. We found that TxlA is a membrane-associated protein, and that it has thioredoxin-like redox activity in vitro. Both the structure and redox function of TxlA are dependent on the C-terminal domain. The results summarized here are described in greater detail in the Ph.D. thesis of Denise Kay, whose training was supported by this grant, and in the three manuscripts attached.
Keywords	Cyanobacteria Photosynthesis Genomics Photoautotrophs Mutants Thioredoxin Synechococcus TxlA PCC 7942
Source Agency	Technical Information Center Oak Ridge Tennessee
Corporate Authors	Department of Energy, Washington, DC.
Document Type	Technical Report
NTIS Issue Number	200622

Novel, Photosynthesis-Associated Thioredoxin-Like Gene.

Novel, Photosynthesis-Associated Thioredoxin-Like Gene.
DE2006850272

Publication Date	2006
Page Count	8
Abstract	We validated much of the previous work on TxlA in PCC 7942, although we have raised doubts about whether the original TxlXg phenotype was actually a homogeneous mutant. We showed that the TxlA homologue in PCC 6803, Sll1980, is required for both photoautotropic and heterotrophic growth. We found that TxlA is a membrane-associated protein, and that it has thioredoxin-like redox activity in vitro. Both the structure and redox function of TxlA are dependent on the C-terminal domain. The results summarized here are described in greater detail in the Ph.D. thesis of Denise Kay, whose training was supported by this grant, and in the three manuscripts attached.
Keywords	Cyanobacteria Photosynthesis Genomics Photoautotrophs Mutants Thioredoxin Synechococcus TxlA PCC 7942
Source Agency	Technical Information Center Oak Ridge Tennessee
Corporate Authors	Department of Energy, Washington, DC.
Document Type	Technical Report
NTIS Issue Number	200622