FEBS Letters | |
The 32 kDa tonoplast polypeptide Di associated with the V0‐type H+‐ATPase of Mesembryanthemum crystallinum L. in the CAM state: A proteolytically processed subunit B? | |
Lüttge, Ulrich2 Ratajczak, Rafael2 Zhigang, An1 Löw, Rainer1 Rausch, Thomas1 | |
[1] Botanisches Institut, Ruprecht-Karls-Universität, Im Neuenheimer Feld 360, D-69120 Heidelberg, Germany;Institut für Botanik, Technische Hoschschule Darmstadt, Schnittspahnstraβe 3-5, D-64287 Darmstadt, Germany | |
关键词: V-type H+-ATPase; Tonoplast; Crassulacean acid metabolism; Protein turnover; Subunit B; Mesembryanthemum crystallinum L; CAM; crassulacean acid metabolism; CHAPS; (3-[3-cholamidopropyl)dimethylammonio]-1-propanesulfonate; PAGE; polyacrylamide gel electrophoresis; PMSF; phenylmethylsulfonyl fluoride; SDS; sodium dodecyl sulfate; | |
DOI : 10.1016/0014-5793(96)00556-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
![]() |
【 摘 要 】
In the facultative halophyte Mesembryanthemum crystallinum, the salt- or age-induced transition to crassulacean acid metabolism (CAM) leads to the occurrence of a tonoplast-bound 32 kDa polypeptide (Di). The alignment of its N-terminal protein sequence with protein sequences of recently cloned higher plant V-ATPase B-subunits indicates that Di may be derived from subunit B by proteolytic removal of a protein fragment of about 20 kDa from its N-terminus. Furthermore, an antiserum directed against Di cross-reacts with subunit B from Nicotiana tabacum. It inhibits both proton pumping and ATP hydrolysis of the holoenzyme in M. crystallinum. As Di remains firmly attached to the holoenzyme the proteolytic processing may have functional implications.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020302942ZK.pdf | 631KB | ![]() |