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Titolo:
Two rice MADS domain proteins interact with OsMADS1
Autore:
Lim, J; Moon, YH; An, G; Jang, SK;
Indirizzi:
Pohang Univ Sci & Technol, Dept Life Sci, Div Mol & Life Sci, Pohang 790784, Kyunghuk, South Korea Pohang Univ Sci & Technol Pohang Kyunghuk South Korea 790784 South Korea
Titolo Testata:
PLANT MOLECULAR BIOLOGY
fascicolo: 4, volume: 44, anno: 2000,
pagine: 513 - 527
SICI:
0167-4412(200011)44:4<513:TRMDPI>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOX GENE FAMILY; MOLECULAR CHARACTERIZATION; TRANSCRIPTION FACTOR; ECTOPIC EXPRESSION; ANTIRRHINUM-MAJUS; FLOWER DEVELOPMENT; WILD-TYPE; ARABIDOPSIS; ACTIVATION; APETALA1;
Keywords:
leucine zipper motif; MADS box; protein-protein interaction; transcriptional activator;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Jang, SK Pohang Univ Sci & Technol, Dept Life Sci, Div Mol & Life Sci, San31, Pohang 790784, Kyunghuk, South Korea Pohang Univ Sci & Technol San 31 Pohang Kyunghuk South Korea 790784
Citazione:
J. Lim et al., "Two rice MADS domain proteins interact with OsMADS1", PLANT MOL B, 44(4), 2000, pp. 513-527

Abstract

OsMADS1 is a MADS box gene controlling flower development in rice. In order to learn more about the function of OsMADS1, we searched for cellular proteins interacting with OsMADS1 employing the yeast two-hybrid system. Two novel proteins with MADS domains, which were named OsMADS14 and OsMADS15, were isolated from a rice cDNA library. OsMADS14 and -15 are highly homologous to the maize MADS box gene ZAP1 which is an orthologue of the floral homeotic gene APETALA1 (AP1). Interactions among the three MADS domain proteinswere confirmed by in vitro experiments using GST-fused OsMADS1 expressed in Escherichia coli and in vitro translated proteins of OsMADS14 and -15. Wedetermined which domains in OsMADS1, -14, and -15 were required for protein-protein interaction employing the two-hybrid system and pull-down experiments. While the K domain was essential for protein-protein interaction, a region preceded by the K domain augmented this interaction. Interestingly, the C-terminal region of OsMADS1 functioned as a transcriptional activation domain in yeast and mammalian cells, while, on the other hand, the C domains of OsMADS14 and -15 exhibited only very weak transcriptional activator functionality, if any at all.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 05:27:01