Detection of Nα-terminally formylated native proteins by a pan-N-formyl methionine-specific antibodyopen access
- Authors
- Kim, Dasom; Seok, Ok-Hee; Ju, Shinyeong; Kim, Sang-Yoon; Kim, Jeong-Mok; Lee, Cheolju; Hwang, Cheol-Sang
- Issue Date
- May-2023
- Publisher
- American Society for Biochemistry and Molecular Biology Inc.
- Keywords
- anti-fMet antibody; fMet/N-degron; mitochondrial methionyl-tRNA formyltransferase; N-formyl methionine; peptide deformylase; protein synthesis
- Citation
- Journal of Biological Chemistry, v.299, no.5, pp.1 - 11
- Indexed
- SCIE
SCOPUS
- Journal Title
- Journal of Biological Chemistry
- Volume
- 299
- Number
- 5
- Start Page
- 1
- End Page
- 11
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/192037
- DOI
- 10.1016/j.jbc.2023.104652
- ISSN
- 0021-9258
- Abstract
- N-formyl methionine (fMet)-containing proteins are produced in bacteria, eukaryotic organelles mitochondria and plastids, and even in cytosol. However, Nα-terminally formylated 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 antibody will be broadly used to enable an understanding of the poorly explored functions and mechanisms of Nt-formylated proteins in various organisms.
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