{The ROXY1 C-Terminal L**}LL Motif Is Essential for the Interaction with TGA Transcription Factors}

Autor(en): Li, Shutian
Gutsche, Nora 
Zachgo, Sabine 
Stichwörter: ARABIDOPSIS; BINDING; DISEASE RESISTANCE; FLORAL ORGAN NUMBER; GLUTAREDOXIN FAMILY; PERIANTHIA GENE; PETAL DEVELOPMENT; Plant Sciences; PROTEIN; REDOX REGULATION; THIOREDOXIN
Erscheinungsdatum: 2011
Herausgeber: AMER SOC PLANT BIOLOGISTS
Journal: PLANT PHYSIOLOGY
Volumen: 157
Ausgabe: 4
Startseite: 2056
Seitenende: 2068
Zusammenfassung: 
{Glutaredoxins (GRXs) are small, ubiquitous, glutathione-dependent oxidoreductases that participate in redox-regulated processes associated with stress responses. Recently, GRXs have been shown to exert crucial functions during flower developmental processes. GRXs modulate their target protein activities by the reduction of protein disulfide bonds or deglutathionylation reactions. The Arabidopsis (Arabidopsis thaliana) GRX ROXY1 participates in petal primordia initiation and further petal morphogenesis. ROXY1 belongs to a land plant-specific class of GRXs with a CC-type active site motif, deviating from the ubiquitously occurring CPYC and CGFS GRX classes. ROXY1 was previously shown to interact with floral TGA transcription factors in the nucleus, and this interaction is a prerequisite for ROXY1 to exert its activity required for Arabidopsis petal development. Deletion analysis further identified the importance of the ROXY1 C terminus for the ROXY1/TGA protein interactions and for the ROXY1 function in petal development. Here, by dissecting the ROXY1 C terminus, an alpha-helical L**}LL motif immediately adjacent to the ROXY1 C-terminal eight amino acids was identified that is essential for the interaction with TGA transcription factors and crucial for the ROXY1 function in planta. Similar to the alpha-helical L**}LL motifs binding to transcriptional coactivators with liganded nuclear receptors in animals, a hydrophobic face formed by the conserved leucines in the L**}LL motif of ROXY1 possibly mediates the interaction with TGA transcription factors. Thus, the alpha-helical L**}LL sequence is a conserved protein-protein interaction motif in both animals and plants. Furthermore, two separate TGA domains were identified by deletion experiments as being essential for mediating TGA protein interactions with ROXYs.}
ISSN: 00320889
DOI: 10.1104/pp.111.185199

Show full item record

Page view(s)

9
Last Week
0
Last month
0
checked on Feb 24, 2024

Google ScholarTM

Check

Altmetric