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Published on August 11, 2006; 10.1104/pp.106.084939

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Received June 9, 2006
Accepted August 2, 2006

Arabidopsis Carboxyl-terminal Domain Phosphatase-like (CPL) Isoforms Share Common Catalytic and Interaction Domains but Have Distinct in Planta Functions

Woo Young Bang , Se Won Kim , Akihiro Ueda , Meenu Vikram , Dae-Jin Yun , Ray A. Bressan , Paul M. Hasegawa , Jeong Dong Bahk *, and Hisashi Koiwa

Department of Molecular Biology, Division of applied Science (BK21 Program) and Environmental Biotechnology National Core Research Center (EBNCRC)
Gyeongsang National University, Jinju 660-701, Korea; and Faculty of Molecular and Environmental Plant Science, Vegetable and Fruit Improvement Center, Department of Horticultural Sciences, 2133 Texas A&M University, College Station, TX 77843-2133, USA
Center for Plant Environmental Stress Physiology, 625 Agriculture Mall Drive, Purdue University, West Lafayette, IN 47907-2010, USA

* Corresponding author; email: jdbahk{at}gsnu.ac.kr.

An Arabidopsis multigene family (predicted to be more than 20 members) encodes plant C-terminal domain (CTD) phosphatases that dephosphorylate serine residues in tandem heptad repeat sequences of the RNA polymerase II C-terminus. CTD phosphatase-like (CPL) isoform 1 and 3 are regulators of osmotic stress and ABA signaling. Evidence presented herein indicates that CPL3 and CPL4 are homologs of a prototype CTD phosphatase, FCP1 (TFIIF-interacting CTD-phosphatase). CPL3 and CPL4 contain catalytic FCP1 homology (FCPH) and breast cancer 1 C-terminus (BRCT) domains. Recombinant CPL3 and CPL4 interact with AtRAP74, an Arabidopsis ortholog of a FCP1-interacting TFIIF subunit. A CPL3 or CPL4 C-terminal fragment that contains the BRCT domain mediates molecular interaction with AtRAP74. Consistent with their predicted roles in transcriptional regulation, GFP-fusion proteins of CPL3, CPL4 and RAP74 all localize to the nucleus. cpl3 mutations that eliminate the BRCT or FCPH domain cause ABA hyper-activation of the stress-inducible RD29a promoter, whereas RNAi suppression of CPL4 results in dwarfism and reduced seedling growth. These results indicate CPL3 and CPL4 are a paralogous pair of general transcription regulators with similar biochemical properties but are required for the distinct developmental and environmental responses. CPL4 is necessary for normal plant growth and thus most orthologous to fungal and metazoan FCP1, whereas CPL3 is an isoform that specifically facilitates ABA-signaling.




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