Kim, Dasom Seok, Ok-Hee Ju, Shinyeong Kim, Sang-Yoon Kim, Jeong-Mok Lee, Cheolju Hwang, Cheol-Sang 2024-01-19T09:32:38Z 2024-01-19T09:32:38Z 2023-06-29 2023-05 0021-9258 https://pubs.kist.re.kr/handle/201004/113737 N-formyl methionine (fMet)-containing proteins are pro-duced in bacteria, eukaryotic organelles mitochondria and plastids, and even in cytosol. However, N alpha-terminally for-mylated proteins have been poorly characterized because of the lack of appropriate tools to detect fMet independently of downstream proximal sequences. Using a fMet-Gly-Ser-Gly-Cys peptide as an antigen, we generated a pan-fMet-specific rabbit polyclonal antibody called anti-fMet. The raised anti-fMet recognized universally and sequence context- independently Nt-formylated proteins in bacterial, yeast, and human cells as determined by a peptide spot array, dot blotting, and immunoblotting. We anticipate that the anti-fMet anti-body will be broadly used to enable an understanding of the poorly explored functions and mechanisms of Nt-formylated proteins in various organisms. English American Society for Biochemistry and Molecular Biology Inc. Detection of Nα-terminally formylated native proteins by a pan-N-formyl methionine-specific antibody Article 10.1016/j.jbc.2023.104652 1 Journal of Biological Chemistry, v.299, no.5 Journal of Biological Chemistry 299 5 Y scie scopus 001009526700001 2-s2.0-85153089298 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article PEPTIDE DEFORMYLASE TRANSFER-RNA SOLUBLE-RNA RECEPTORS INITIATOR FORMYLTRANSFERASE EXPRESSION MECHANISM RIBOSOME PLATFORM