PubMed · 1653812
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S Tsuiki, A Hiraga. 1991. [Structure and function of protein phosphatases].. https://pubmed.ncbi.nlm.nih.gov/1653812/
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Differently phosphorylated forms of RNA polymerase (Pol) II are required to guide the enzyme through the transcription cycle. Here, we show that a phosphorylation/dephosphorylation cycle is also important for RNA polymerase I-dependent synthesis of rRNA precursors. A key component of the Pol II transcription system is Fcp1p, a phosphatase that dephosphorylates the C-terminal domain of the largest Pol II subunit. Fcp1p stimulates transcription elongation and is required for Pol II recycling after transcription termination. We found that Fcp1p is also part of the RNA Pol I transcription apparatus. Fcp1p is required for efficient rDNA transcription in vivo, and also, recombinant Fcp1p stimulates rRNA synthesis both in promoter-dependent and in nonspecific transcription assays in vitro. We demonstrate that Fcp1 activity is not involved in the formation of the initiation-active form of Pol I (the Pol I-Rrn3p complex) and propose that dephosphorylation of Pol I by Fcp1p facilitates chain elongation during rRNA synthesis.
Phosphorylation and dephosphorylation of a protein often serve as an "on-and-off" switch in the regulation of cellular activities. Recent studies demonstrate the involvement of protein phosphorylation in almost all signaling pathways in plants. A significant portion of the sequenced Arabidopsis genome encodes protein kinases and protein phosphatases that catalyze reversible phosphorylation. For optimal regulation, kinases and phosphatases must strike a balance in any given cell. Only a very small fraction of the thousands of protein kinases and phosphatases in plants has been studied experimentally. Nevertheless, the available results have demonstrated critical functions for these enzymes in plant growth and development. While serine/threonine phosphorylation is widely accepted as a predominant modification of plant proteins, the function of tyrosine phosphorylation, desptie its overwhelming importance in animal systems, had been largely neglected until recently when tyrosine phosphatases (PTPs) were characterized from plants. This review focuses on the structure, regulation, and function of protein phosphatases in higher plants.
For many years, the regulation of protein structure and function by phosphorylation and dephosphorylation was considered a relatively recent invention that arose independently in each phylogenetic domain. Over time, however, incidents of apparent domain trespass involving the presence of 'eukaryotic' protein kinases or protein phosphatases in prokaryotic organisms were reported with increasing frequency. Today, genomics has provided the means to examine the phylogenetic distribution of 'eukaryotic' protein kinases and protein phosphatases in a comprehensive and systematic manner. The results of these genome searches challenge previous conceptions concerning the origins and evolution of this versatile regulatory mechanism.