Abstract
Chloroplast ATP-synthase (CF1) subunit delta (δ) has been isolated from spinach thylakoids in the presence of SDS. By automated Edman degradation and online analysis of PTH derivatives the 35 N-terminal amino acid residues were sequenced. The mature protein starts with: NH2-Val-Asp-Ser-Thr-Ala-Ser-Arg-Tyr-Ala-. This protein sequence allows alignment of spinach δ with the sequences of Z. mays 25 kDa polypeptide, the δ subunit of Rps. blastica, Rsp. rubrum and E. coli F1, and of bovine OSCP, but not with mitochondrial δ. Secondary structure calculations and helical wheel plots reveal a conserved secondary structure. The analyzed N-terminal sequences probably build a short amphipathic alpha helix with two adjacent turns. The such aligned polar residues around Tyr8 of subunit δ are suitable to channel protons.
Dates
Type | When |
---|---|
Created | 7 years ago (Aug. 2, 2018, 1:49 p.m.) |
Deposited | 4 years, 2 months ago (June 22, 2021, 5:37 p.m.) |
Indexed | 2 years, 7 months ago (Jan. 5, 2023, 9:19 p.m.) |
Issued | 37 years, 8 months ago (Dec. 1, 1987) |
Published | 37 years, 8 months ago (Dec. 1, 1987) |
Published Online | 11 years, 2 months ago (June 2, 2014) |
Published Print | 37 years, 8 months ago (Dec. 1, 1987) |
@article{Berzborn_1987, title={Protein Sequence and Structure of N-terminal Amino Acids of Subunit Delta of Spinach Photosynthetic ATP-Synthase CF1}, volume={42}, ISSN={0939-5075}, url={http://dx.doi.org/10.1515/znc-1987-11-1215}, DOI={10.1515/znc-1987-11-1215}, number={11–12}, journal={Zeitschrift für Naturforschung C}, publisher={Walter de Gruyter GmbH}, author={Berzborn, Richard J. and Finke, Werner and Otto, Joachim and Meyer, Helmut E .}, year={1987}, month=dec, pages={1231–1238} }