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The 32 kDa tonoplast polypeptide D i associated with the V0-type H +-ATPase of Mesembryanthemum crystallinum L. in the CAM state: A proteolytically processed subunit B?

Zhigang, An ; Löw, Rainer ; Rausch, Thomas ; Lüttge, Ulrich ; Ratajczak, Rafael

FEBS letters, 1996-07, Vol.389 (3), p.314-318 [Periódico revisado por pares]

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Título:
The 32 kDa tonoplast polypeptide D i associated with the V0-type H +-ATPase of Mesembryanthemum crystallinum L. in the CAM state: A proteolytically processed subunit B?
Autor: Zhigang, An ; Löw, Rainer ; Rausch, Thomas ; Lüttge, Ulrich ; Ratajczak, Rafael
Assuntos: Crassulacean acid metabolism ; Mesembryanthemum crystallinum L ; Protein turnover ; Subunit B ; Tonoplast ; V-type H +-ATPase
É parte de: FEBS letters, 1996-07, Vol.389 (3), p.314-318
Descrição: 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 (D i). The alignment of its N-terminal protein sequence with protein sequences of recently cloned higher plant V-ATPase B-subunits indicates that D i 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 D i cross-reacts with subunit B from Nicotiana tabacum. It inhibits both proton pumping and ATP hydrolysis of the holoenzyme in M. crystallinum. As D i remains firmly attached to the holoenzyme the proteolytic processing may have functional implications.
Editor: Elsevier B.V
Idioma: Inglês

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