2.1.1.310: 25S rRNA (cytosine2870-C5)-methyltransferase
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For detailed information about 25S rRNA (cytosine2870-C5)-methyltransferase, go to the full flat file.
Reaction
Synonyms
m5C-methyltransferase, NOP2, NSUN1/Nol1, p120, proliferation-associated nucleolar antigen, protein p120, RNA:m5C-MTase
ECTree
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Engineering
Engineering on EC 2.1.1.310 - 25S rRNA (cytosine2870-C5)-methyltransferase
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C478A
additional information
the polysome profile from the mutant reveals defect in 60S biogenesis and significant reduction in polysome fractions compared with isogenic wild type
C478A
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the polysome profile from the mutant reveals defect in 60S biogenesis and significant reduction in polysome fractions compared with isogenic wild type
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generation of GFP-tagged chimeric protein formed by yeast Nop2 and p120 fragments. The HYB protein, which is composed of N-terminal Nop2 and C-terminal p120 domains, efficiently localizes within the nucleolus, demonstrating that all necessary cell sorting signals are indeed located in the Nop2 N-terminal domain
additional information
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functional complementation of Nop2-deficient yeasts by human protein p120, the N-terminal domain of Nop2 is essential for efficient complementation by p120 in yeast. Generation of GFP-tagged chimeric protein formed by Nop2 and human p120 fragments. The HYB protein, which is composed of N-terminal Nop2 and C-terminal p120 domains, efficiently localizes within the nucleolus, demonstrating that all necessary cell sorting signals are indeed located in the Nop2 N-terminal domain. The yeast strain expressing N-terminal domain-truncated Nop2 is not viable, indicating that localization of Nop2 is important for its function. A double mutant of Nop2 protein with two mutated cysteines that are expected to be involved in catalysis, namely Cys424 and Cys478, shows no phenotype
additional information
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functional complementation of Nop2-deficient yeasts by human protein p120, the N-terminal domain of Nop2 is essential for efficient complementation by p120 in yeast. Generation of GFP-tagged chimeric protein formed by Nop2 and human p120 fragments. The HYB protein, which is composed of N-terminal Nop2 and C-terminal p120 domains, efficiently localizes within the nucleolus, demonstrating that all necessary cell sorting signals are indeed located in the Nop2 N-terminal domain. The yeast strain expressing N-terminal domain-truncated Nop2 is not viable, indicating that localization of Nop2 is important for its function. A double mutant of Nop2 protein with two mutated cysteines that are expected to be involved in catalysis, namely Cys424 and Cys478, shows no phenotype
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