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KIX domain of AtMed15a, a Mediator subunit of Arabidopsis, is required for its interaction with different proteins.


ABSTRACT: Med15 is an important subunit of Mediator Tail module and is characterized by a KIX domain present towards amino terminal. In yeast and metazoans, Med15 KIX domain has been found to interact with various transcription factors regulating several processes including carbohydrate metabolism, lipogenesis, stress response and multidrug resistance. Mechanism of Med15 functioning in Arabidopsis is largely unknown. In this study, interactome of KIX domain of Arabidopsis Med15, AtMed15a, was characterized. We found 45 proteins that interact with AtMed15a KIX domain, including 11 transcription factors, 3 single strand nucleic acid-binding proteins and 1 splicing factor. The third helix of the KIX domain was found to be involved in most of the interactions. Mapping of the regions participating in the interactions revealed that the activation domain of a transcription factor, UKTF1 interacted with AtMed15a KIX domain. Thus, our results suggest that in Arabidopsis, activation domain of transcription factors target KIX domain of AtMed15a for their transcriptional responses.

SUBMITTER: Kumar V 

PROVIDER: S-EPMC5846557 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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KIX domain of AtMed15a, a Mediator subunit of Arabidopsis, is required for its interaction with different proteins.

Kumar Vinay V   Waseem Mohd M   Dwivedi Nidhi N   Maji Sourobh S   Kumar Angad A   Thakur Jitendra K JK  

Plant signaling & behavior 20180208 2


Med15 is an important subunit of Mediator Tail module and is characterized by a KIX domain present towards amino terminal. In yeast and metazoans, Med15 KIX domain has been found to interact with various transcription factors regulating several processes including carbohydrate metabolism, lipogenesis, stress response and multidrug resistance. Mechanism of Med15 functioning in Arabidopsis is largely unknown. In this study, interactome of KIX domain of Arabidopsis Med15, AtMed15a, was characterize  ...[more]

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