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
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
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