A novel motif at the C-terminus of palmitoyltransferases is essential for Swf1 and Pfa3 function in vivo

GONZÁLEZ MONTORO, AYELÉN; QUIROGA, RODRIGO; MACCIONI, HUGO J F; VALDEZ TAUBAS, JAVIER

PORTLAND PRESS LTD

Año: 2009 vol. 419 p. 301 - 301

meta content="1" name="qrichtext" /> p, li { white-space: pre-wrap; } S-acylation (commonly known as palmitoylation) is a widespread post-translational modification that consists of the addition of a lipid molecule to cysteine residues of a protein through a thioester bond. This modification is predominantly mediated by a family of proteins referred to as PATs (palmitoyltransferases). Most PATs are polytopic membrane proteins, with four to six transmembrane domains, a conserved DHHC motif and variable C-and N-terminal regions, that are probably responsible for conferring localization and substrate specificity. There is very little additional information on the structure-function relationship of PATs. Swf1 and Pfa3 are yeast members of the DHHC family of proteins. Swf1 is responsible for the S-acylation of several transm