Results 171 to 180 of about 9,732 (194)
Interaction study of MADS-domain proteins in tomato [PDF]
Journal of Experimental Botany, 2008 MADS-domain proteins are important transcription factors involved in many biological processes of plants. Interactions between MADS-domain proteins are essential for their functions. In tomato (Solanum lycopersicum), the number of MIKC(c)-type MADS-domain proteins identified has totalled 36, but a large-scale interaction assay is lacking. In this study,
Melvin Duvall +2 more
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The ‘ABC’ of MADS domain protein behaviour and interactions
Seminars in Cell and Developmental Biology, 2010Development of eudicot flowers is under tight developmental control by genes belonging to the MADS box transcription factor family, as is nicely represented by the well-known ABC model of floral organ development. During the last two decades enormous progress has been made in our understanding of the molecular mechanisms underlying the combinatorial ...
Kerstin Kaufmann +2 more
exaly +3 more sources
Molecular mechanisms of floral organ specification by MADS domain proteins
Current Opinion in Plant Biology, 2016Flower development is a model system to understand organ specification in plants. The identities of different types of floral organs are specified by homeotic MADS transcription factors that interact in a combinatorial fashion. Systematic identification of DNA-binding sites and target genes of these key regulators show that they have shared and unique ...
Kerstin Kaufmann +2 more
exaly +5 more sources
Mapping the protein regions responsible for the functional specificities of the Arabidopsis MADS domain organ-identity proteins. [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 1996 The Arabidopsis MADS domain proteins AP1, AP3, PI, and AG specify floral organ identity. All of these proteins contain a MADS domain required for DNA binding and dimerization; a region termed L (linker between MADS domain and K domain), which plays an important role in dimerization specificity; the K domain, named for its similarity to the coiled-coil ...
Elliot Meyerowitz, Meyerowitz Elliot M
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Plant Molecular Biology, 2004
The MADS proteins APETALA3 (AP3), PISTILLATA (PI), SEPALLATAI (SEPI), SEP2, SEP3, AGAMOUS, and APETALA are required for proper floral organ identity in Arabidopsis flowers. All of these floral MADS proteins conserve two domains: the MADS domain that mediates DNA binding and dimerization, and the K domain that mediates protein protein interaction. The K
Thomas Jack, Jack Thomas
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The MADS proteins APETALA3 (AP3), PISTILLATA (PI), SEPALLATAI (SEPI), SEP2, SEP3, AGAMOUS, and APETALA are required for proper floral organ identity in Arabidopsis flowers. All of these floral MADS proteins conserve two domains: the MADS domain that mediates DNA binding and dimerization, and the K domain that mediates protein protein interaction. The K
Thomas Jack, Jack Thomas
exaly +3 more sources
Plant Journal, 1997
SummaryMADS domain (for MCM1, AG, DEFA and SRF) proteins are regulatory proteins found in all major eukaryotic kingdoms. Plant MADS domain regulatory proteins have a region of moderate sequence similarity that has been designated as the K domain, and its predicted coiled‐coil structure suggests a role in establishing a protein—protein interaction.
Hong Ma
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SummaryMADS domain (for MCM1, AG, DEFA and SRF) proteins are regulatory proteins found in all major eukaryotic kingdoms. Plant MADS domain regulatory proteins have a region of moderate sequence similarity that has been designated as the K domain, and its predicted coiled‐coil structure suggests a role in establishing a protein—protein interaction.
Hong Ma
exaly +3 more sources
Two rice MADS domain proteins interact with OsMADS1
Plant Molecular Biology, 2000OsMADS1 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.
Lim, J, Moon, YH, An, G, Jang, SK
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Dimerization specificity of Arabidopsis MADS domain homeotic proteins APETALA1, APETALA3, PISTILLATA, and AGAMOUS. [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 1996 The MADS domain homeotic proteins APETALA1 (AP1), APETALA3 (AP3), PISTILLATA (PI), and AGAMOUS (AG) act in a combinatorial manner to specify the identity of Arabidopsis floral organs. The molecular basis for this combinatorial mode of action was investigated.
Elliot Meyerowitz, Meyerowitz Elliot M
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MADS domain proteins in plant development.
Biological chemistry, 1997© 1997 Walter de Gruyter GmbH.
Riechmann, José Luis +1 more
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Gene, 2005
MIKC-type proteins represent a class of MADS-domain transcription factors and are defined by a unique domain structure: in addition to the highly conserved DNA-binding MADS-domain, they have three other domains ('I', 'K' and 'C'), with the keratin-like K-domain being the most highly conserved and characteristic one.
Kerstin Kaufmann +2 more
exaly +3 more sources
MIKC-type proteins represent a class of MADS-domain transcription factors and are defined by a unique domain structure: in addition to the highly conserved DNA-binding MADS-domain, they have three other domains ('I', 'K' and 'C'), with the keratin-like K-domain being the most highly conserved and characteristic one.
Kerstin Kaufmann +2 more
exaly +3 more sources