Apple aminopropyl transferase, MdACL5 interacts with putative elongation factor 1-alpha and S-adenosylmethionine synthase [corrected].
Biochem Biophys Res Commun
; 366(1): 162-7, 2008 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-18053797
ABSTRACT
Several lines of evidence suggest different allocations of the physiological roles of aminopropyl transferase genes, SPMS and ACL5 in plants. To get deeper insights into the physiological role of apple ACL5 (MdACL5), we performed yeast two-hybrid (Y2H) assay to identify proteins which interact with MdACL5. After intense screening processes, including the swapping of the bait and prey vectors and in vitro coimmunoprecipitation, we identified three MdACL5-interacting proteins putative translation elongation factor 1A (eEF-1A), putative S-adenosyl-l-methionine synthetase (SAMS) and an unknown protein. Results from Y2H and RNA gel blot analysis suggested the involvement of MdACL5 and eEF-1A or SAMS complexes in the plant growth and development of the organized tissues and/or organs.
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Base de dados:
MEDLINE
Assunto principal:
Espermidina Sintase
/
Fator 1 de Elongação de Peptídeos
/
Malus
/
Mapeamento de Interação de Proteínas
/
Metionina Adenosiltransferase
/
Complexos Multienzimáticos
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article