Hey you !
Are you ready to learn a bit more about a gene superfamily?
Today we will talk about Thioredoxins (TRX), that is class of small proteins characterized for a short sequence of four amino acids (Cys–Xxx–Xxx–Cys)* at their active site. TRX were identified in 1964 in bacterium Escherichia coli, and ever since it has been widely studied.
Thioredoxins are important molecules involved mainly in the control of cellular reduction/oxidation (redox) balance. Therefore, they are related to oxidative stress and different types of cancer cases, usually showing an elevated expression. The two cysteines (Cys) residues presents in the conserved active site sequence work as an intracellular reductase by a dithiol/disulfide exchange and are responsible for their redox activity. TRX also is associated with others biological processes as gene expression and signal transduction in all organisms.
In our analysis Pterygoplichthys transcriptome, we found 3 differents types of TXN (TMX, TXN and TXNDC) but they have practically the same functions. The basic difference is the local where are expressed and found in cell. The most abundant of those types in the transcriptome of Pterygoplichthys was TXNDC, with 13 distinct transcripts.
Got interested in Thioredoxins? Learn more with this nice review: Multiple catalytically active thioredoxin folds: a winning strategy for many functions .
*Cys - amino acid cysteine
Xxx - some amino acid