Co- and post-translational modifications in Rubisco: unanswered questions

Co- and post-translational modifications in Rubisco: unanswered questions.

Both the large (LS) and small (SS) subunits of Rubisco are subject to a plethora of co- and post-translational modifications. With the exceptions of LS carbamylation and SS transit sequence processing, the remaining modifications, including deformylation, acetylation, methylation, and N-terminal proteolytic processing of the LS, are still biochemically and/or functionally undefined although the...

Translation and post-translational modifications in Plasmodium

Malaria is one of the most important human parasitic diseases in the world, affecting about 400 million people and killing about 1 million children every year. Our relationship with the malarial parasite has been a long one on the evolutionary scale, and the methods adopted by the parasite to thrive and colonize our bodies are truly fascinating. In order to control the disease, it is of fundame...

Post-translational modifications of tubulin

Microtubules are the largest filamentous components of the eukaryotic cytoskeleton. In spite of their extraordinary level of structural conservation, microtubules fulfill a vast range of different functions in cells. How this functional diversity is achieved remains an open question; however, recent advances point towards post-translational modifications (PTMs) of tubulin as a potent mechanism ...

E-Learning: some unanswered questions

Post-translational modifications in nitrile hydratase family

Fe-type nitrile hydratase (NHase) from Rhodococcus sp. N771 has a novel non-heme iron active center with two post-translationally modified cysteine residues, cysteine-sulfenic and -sulfinic acids. The modified residues are involved in the sequence motif, Cys-Xxx-Leu-Cys-Ser-Cys (Xxx = Ser(Fetype)/Thr(Co-type)), which is conserved among all known NHases as well as in the homologous enzyme, thioc...