MALDI-MS Analysis of Peptide Libraries Expands the Scope of Substrates for Farnesyltransferase.

ABSTRACT: Protein farnesylation is a post-translational modification where a 15-carbon farnesyl isoprenoid is appended to the C-terminal end of a protein by farnesyltransferase (FTase). This modification typically causes proteins to associate with the membrane and allows them to participate in signaling pathways. In the canonical understanding of FTase, the isoprenoids are attached to the cysteine residue of a four-amino-acid CaaX box sequence. However, recent work has shown that five-amino-acid sequences can be recognized, including the pentapeptide CMIIM. This paper describes a new systematic approach to discover novel peptide substrates for FTase by combining the combinatorial power of solid-phase peptide synthesis (SPPS) with the ease of matrix-assisted laser desorption ionization-mass spectrome

SUBMITTER: Schey GL 

PROVIDER: S-EPMC8584866 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature