Autor: |
Hoesche JA; Department of Biology, Lehrstuhl Biochemie der Pflanzen, Ruhr-Universität Bochum, Germany., Berzborn RJ |
Jazyk: |
angličtina |
Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 1992 Dec 29; Vol. 1171 (2), pp. 201-4. |
DOI: |
10.1016/0167-4781(92)90121-f |
Abstrakt: |
lambda gt10 cDNA clones for the nuclear encoded subunit delta of chloroplast ATP-synthase from Pisum sativum have been isolated. The 5' end was completed by PCR. The sequenced cDNA codes for the import precursor. N-Terminal sequencing of the mature protein isolated from chloroplasts revealed that the processing sites of the transit peptide from Pisum sativum and Spinacea oleracea are similar. The overall homology of the deduced amino acid sequences of the mature delta proteins from higher plants is about 40%. The conservation among hydrophilic residues is higher than for hydrophobic ones, indicating that the surface of delta is important for its function within the ATP-synthase. |
Databáze: |
MEDLINE |
Externí odkaz: |
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