Transglutaminase 5 is acetylated at the N-terminal end.
Transglutaminases (TGases) are calcium-dependent enzymes that catalyse cross-linking between proteins by acyl transfer reaction; they are involved in many biological processes including coagulation, differentiation, and tissue repair. Transglutaminase 5 was originally cloned from keratinocytes, and a partial biochemical characterisation showed its involvement in skin differentiation, in parallel to TGase 1 and TGase 3. Here, we demonstrate, by electrospray tandem mass spectrometry that TGase 5 is acetylated at the N-terminal end. Moreover, in situ measurement of TGase activity shows that endogenous TGase 5 is active upon treatment with phorbol acetate, and the enzyme co-localises with vimentin intermediate filaments.
Biochemistry Laboratory, IDI-IRCCS, University of Rome Tor Vergata, Rome, Italy.
A
A
Rufini
F
F
Vilbois
A
A
Paradisi
S
S
Oddi
R
R
Tartaglione
A
A
Leta
G
G
Bagetta
P
P
Guerrieri
A
A
Finazzi-Agro'
G
G
Melino
E
E
Candi
D000107:Acetylation; D000818:Animals; D002478:Cells, Cultured; D006801:Humans; D007382:Intermediate Filaments / Q000378:metabolism; D015603:Keratinocytes / Q000166:cytology / Q000378:metabolism; D013058:Mass Spectrometry; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011503:Transglutaminases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014746:Vimentin / Q000378:metabolism
D011994:Recombinant Proteins; D014746:Vimentin; C418703:transglutaminase 5; D011503:Transglutaminases