Isolation and characterization of two Brassica napus embryo acyl-ACP thioesterase cDNA clones
In: Plant molecular biology, Jg. 23 (1993), Heft 4, S. 769-778
Online
academicJournal
- print, 25 ref
Zugriff:
Acyl-ACP thioesterases (EC 3.1.2.14) are involved in regulating chain termination of fatty acid biosynthesis in plant systems. Previously, acyl-ACP thioesterase purified from Brassica napus seed tissue has been shown to have a high preference for hydrolysing oleoyl-ACP. Here, oligonucleotides derived from B. napus oleoyl-ACP thioesterase protein sequence data have been used to isolate two acyl-ACP thioesterase clones from a B. napus embryo cDNA library. The two clones, pNL2 and pNL3, contain 1642 bp and 1523 bp respectively and differ in the length of their 3' non-coding regions. Both cDNAs contain open reading frames of 366 amino acids which encode for 42 kDa polypeptides. Mature rape thioesterase has an apparent molecular weight of 38 kDa on SDS-PAGE and these cDNAs therefore encode for precursor forms of the enzyme.
Titel: |
Isolation and characterization of two Brassica napus embryo acyl-ACP thioesterase cDNA clones
|
---|---|
Autor/in / Beteiligte Person: | LOADER, N. M ; WOOLNER, E. M ; HELLYER, A ; SLABAS, A. R ; SAFFORD, R |
Link: | |
Zeitschrift: | Plant molecular biology, Jg. 23 (1993), Heft 4, S. 769-778 |
Veröffentlichung: | Dordrecht: Springer, 1993 |
Medientyp: | academicJournal |
Umfang: | print, 25 ref |
ISSN: | 0167-4412 (print) |
Schlagwort: |
|
Sonstiges: |
|