Pin1At encoding a peptidyl-prolyl cis/trans isomerase regulates flowering time in Arabidopsis.
Floral transition in plants is regulated by an integrated network of flowering genetic pathways. We show that an Arabidopsis PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SUPPRESSOR OF OVEREXPRESSION OF CO 1 (SOC1) and AGAMOUS-LIKE 24 (AGL24). Pin1At regulates flowering, which is genetically mediated by AGL24 and SOC1. Pin1At interacts with the phosphorylated AGL24 and SOC1 in vitro and with AGL24 and SOC1 in vivo and accelerates the cis/trans conformational change of phosphorylated Ser/Thr-Pro motifs of AGL24 and SOC1. We further demonstrate that these Ser/Thr-Pro motifs are important for Pin1At function in promoting flowering through AGL24 and SOC1 and that the interaction between Pin1At and AGL24 mediates the AGL24 stability in the nucleus. Taken together, we propose that phosphorylation-dependent prolyl cis/trans isomerization of key transcription factors is an important flowering regulatory mechanism.
Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore.
Yu
Y
Wang
Chang
C
Liu
Daiwen
D
Yang
Hao
H
Yu
Yih-Cherng
YC
Liou
D020816:Amino Acid Motifs; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D035264:Flowers / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D026161:MADS Domain Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D010766:Phosphorylation; D017440:Photoperiod; D055550:Protein Stability
C419046:AGL20 protein, Arabidopsis; C478065:AGL24 protein, Arabidopsis; D029681:Arabidopsis Proteins; D026161:MADS Domain Proteins; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; C000606847:PIN1AT protein, Arabidopsis; D019696:Peptidylprolyl Isomerase