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.