Abstract
Peptide deformylase (DEF; EC 3.5.1.88) removes the N-formyl group from nascent polypeptides. Two nuclear-encoded DEFs in Arabidopsis thaliana (At) are localized to chloroplasts, and thus, the N-termini of chloroplast-translated proteins may be a consequence of AtDEFs3 substrate specificity. Using peptide analogs of select chloroplast-translated proteins, AtDEF1 activity was as much as 100-fold lower than AtDEF2 activity and showed little variance with peptide sequence. However, AtDEF2 activity was significantly influenced by peptide sequence, with the most efficiently processed substrate mimicking the N-terminus of the nascent D1 polypeptide, a core protein of photosystem II. Though AtDEF23s specificity was predictive of N-formyl retention for some chloroplast proteins, exceptions suggests that additional factors in vivo aid in determining the retention of an N-formyl group.
| Original language | English |
|---|---|
| Pages (from-to) | 135-141 |
| Number of pages | 7 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 406 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2002 |
Bibliographical note
Funding Information:We are grateful for funding provided by the Department of Energy Grant DEFG02-92ER20075 to R.L.H. and by the Tobacco and Health Research Institute Grant 5-41176 to M.A.W., L.M.A.D., and R.L.H.
Funding
We are grateful for funding provided by the Department of Energy Grant DEFG02-92ER20075 to R.L.H. and by the Tobacco and Health Research Institute Grant 5-41176 to M.A.W., L.M.A.D., and R.L.H.
| Funders | Funder number |
|---|---|
| Tobacco and Health Research Institute | 5-41176 |
| Michigan State University-U.S. Department of Energy (MSU-DOE) Plant Research Laboratory | DEFG02-92ER20075 |
Keywords
- ATPase
- Arabidopsis thaliana
- Chloroplast
- D1
- N-terminal processing
- Peptide deformylase
- Rubisco
- Specificity
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology