Sequence analysis and characterization of vacuolar-type H+ -ATPase proteolipid transcript from Acanthus ebracteatus Vah1.
The vacuolar-type H+ -ATPase (V-ATPase) is a multimeric enzyme with diverse functions in plants such as nutrient transport, flowering, stress tolerance, guard cell movement and development. A partial sequence of V-ATPase proteolipid was identified among the expressed sequence tags (ESTs) generated from Acanthus ebracteatus, and selected for full-length sequencing. The 876-nucleotide cDNA consists of an open reading frame of 165 amino acids. The deduced amino acid sequence displays high similarity (81%) with its homologs from Arabidopsis thaliana, Avecinnia marina and Gossypium hirsutum with the four transmembrane domains characteristics of the 16 kDa proteolipid subunit c of V-ATPase well conserved in this protein. Southern analysis revealed the existence of several members of proteolipid subunit c of V-ATPase in A. ebracteatus. The mRNA of this gene was detected in leaf, floral, stem and root tissues, however, the expression level was lower in stem and root tissues.
Ho
Chai-Ling
CL
Department of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia. clho@biotech.upm.edu.my
Nguyen
Phuoc Dang
PD
Harikrishna
Jennifer Ann
JA
Rahim
Raha Abdul
RA
D027901:Acanthaceae / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics*; D011510:Proteolipids / Q000737:chemistry / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics*; D017422:Sequence Analysis, DNA; D020539:Sequence Analysis, Protein; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics*; D014617:Vacuoles / Q000201:enzymology / Q000235:genetics
D010940:Plant Proteins; D011510:Proteolipids; D012333:RNA, Messenger; D025262:Vacuolar Proton-Translocating ATPases