Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential Ser-5-specific C-terminal domain phosphatases Journal Article
| Authors: | Koiwa, H.; Hausmann, S.; Bang, W. Y.; Ueda, A.; Kondo, N.; Hiraguri, A.; Fukuhara, T.; Bahk, J. D.; Yun, D. J.; Bressan, R. A.; Hasegawa, P. M.; Shuman, S. |
| Article Title: | Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential Ser-5-specific C-terminal domain phosphatases |
| Abstract: | Transcription and mRNA processing are regulated by phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II, which consists of tandem repeats of a Y1S2P3T 4S5P6S7 heptapeptide. Previous studies showed that members of the plant CTD phosphatase-like (CPL) protein family differentially regulate osmotic stress-responsive and abscisic acid-responsive transcription in Arabidopsis thaliana. Here we report that AtCPL1 and AtCPL2 specifically dephosphorylate Ser-5 of the CTD heptad in Arabidopsis RNA polymerase II, but not Ser-2. An N-terminal catalytic domain of CPL1, which suffices for CTD Ser-5 phosphatase activity in vitro, includes a signature DXDXT acylphosphatase motif, but lacks a breast cancer 1 CTD, which is an essential component of the fungal and metazoan Fcp1 CTD phosphatase enzymes. The CTD of CPL1, which contains two putative double-stranded RNA binding motifs, is essential for the in vivo function of CPL1 and includes a C-terminal 23-aa signal responsible for its nuclear targeting. CPL2 has a similar domain structure but contains only one double-stranded RNA binding motif. Combining mutant alleles of CPL1 and CPL2 causes synthetic lethality of the male but not the female gametes. These results indicate that CPL1 and CPL2 exemplify a unique family of CTD Ser-5-specific phosphatases with an essential role in plant growth and development. |
| Keywords: | unclassified drug; gene deletion; nonhuman; genetic analysis; protein domain; protein function; allele; serine; carboxy terminal sequence; in vitro study; enzyme activity; structure activity relation; transcription factors; rna-binding proteins; molecular sequence data; amino terminal sequence; recombinant fusion proteins; substrate specificity; cellular distribution; protein structure, tertiary; cell nucleus; protein dephosphorylation; rna polymerase ii; fungus; fungi; rna binding; lethality; mutant; double stranded rna; enzyme active site; phosphoprotein phosphatase; metazoa; arabidopsis; arabidopsis thaliana; arabidopsis proteins; gamete; metazoon; arabidopsis protein; plants, genetically modified; priority journal; article; acylphosphatase; phosphatase like protein 1; phosphatase like protein 2 |
| Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
| Volume: | 101 |
| Issue: | 40 |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Date Published: | 2004-10-05 |
| Start Page: | 14539 |
| End Page: | 14544 |
| Language: | English |
| DOI: | 10.1073/pnas.0403174101 |
| PROVIDER: | scopus |
| PMCID: | PMC521950 |
| PUBMED: | 15388846 |
| DOI/URL: | |
| Notes: | Proc. Natl. Acad. Sci. U. S. A. -- Cited By (since 1996):41 -- Export Date: 16 June 2014 -- CODEN: PNASA -- Molecular Sequence Numbers: GENBANK: AY557186, AY557187; -- Source: Scopus |
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