—Acetoacetyl-CoA thiolase (AACT, β-ketothiolase) is an enzyme that catalyzes the biological Claisen condensation of two molecules of acetyl-CoA to form acetoacetyl-CoA. In plants, AACT is known to be involved in the early step of mevalonate pathway which is essential in producing isoprenoid compounds such as sterols, carotenoids and growth regulators. In order to study this gene, we attempt to clone the gene from oil palm. The AACT gene was cloned from a genomic library of oil palm using a homologous probe from the AACT cDNA clone. The probe is consisted of 1.5 kb in length. A fragment of 12 470 bp was successfully sequenced and contains nine exons interrupted by eight introns. This fragment represented 886 bp in length or 59 % of 1247 bp of the putative AACT mRNA sequence. Transcription start site (TSS) and its regulatory regions were predicted at the 5’-flanking region of this gene. Three TSS points, at positions -1284, -1283 and -280 from the putative start codon were identified. The binding sites for GT-1 element, SBF-1 and sequences resembling the binding sites of several other transcription factors were also identified.
—β-ketothiolase, enzyme, mevalonate pathway, polyhydrohybutyrate (PHB), regulatory regions.
Khadijah Hanim Abdul Rahman is with the School of Bioprocess Engineering, Universiti Malaysia Perlis, 01000 Kangar, Perlis, Malaysia (e-mail: firstname.lastname@example.org).
Mohd Razip Samian is with School of Biological Sciences, Universiti Sains Malaysia, 11200 Gelugor, Penang, Malaysia (e-mail: email@example.com).
Cite:Khadijah Hanim Abdul Rahman and Mohd Razip Samian, "Cloning and Promoter Identification of Acetoacetyl-CoA Thiolase Gene from Oil Palm, Elaeis guineensis Jacq.," International Journal of Environmental Science and Development vol. 5, no. 4, pp. 362-366, 2014.