By Fuyuhiko Tamanoi, Steven G. Clarke
Protein methylation has lately emerged as probably the most intriguing components of research on posttranslational amendment. a wide kin of protein methyltransferases has been pointed out and their structural homes were characterised. those stories have supplied novel insights into how methylation regulates various organic capabilities together with DNA and RNA metabolism, protein synthesis and sign transduction. Methylation additionally performs very important roles in getting older. This quantity is meant to seize those fresh advancements touching on protein methyltransferases.
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Protein methylation has lately emerged as probably the most interesting parts of analysis on posttranslational amendment. a wide family members of protein methyltransferases has been pointed out and their structural houses were characterised. those stories have supplied novel insights into how methylation regulates quite a few organic features together with DNA and RNA metabolism, protein synthesis and sign transduction.
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Extra resources for Protein Methyltransferases
The existence of this PRMTl-like molecule has been noted [20, 36], although the unique N-terminal region of 76 amino acids was only recently recognized. This N-terminal region is conserved between mouse and man, and an orthologue also exists in fish (fuguL3) . The unique N-terminal end harbors a functional myristoylation motif that facilitates its association with the plasma membrane. The second singular property of PRMT8 is its tissue-specific expression pattern (it is largely expressed in the brain).
2). Recently, the yeast ribosomal protein LI2 was identified as a specific substrate for Rmt2p . A single 5-A^-monomethylarginine was identified in LI2 in the sequence, IQNRQAA. Therefore, Rmt2p does not methylate a GAR motif as Rmtlp/Hmtlp does. It is unclear if there is a mammalian orthologue of Rmt2p, and 8-A^-monomethylarginine has not yet been detected in higher eukaryotes. C. HSL7 The predominant type II protein arginine methyltransferase in Saccharomyces cerevisiae, HslTp (Histone synthetic-lethal 7), was identified because of its homology to PRMT5 [64, 99].
BEDFORD 69. , Vishwanath, S. , and Sif, S. (2004). Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol 24:9630-9645. 70. Friesen, W. , Wyce, A. and Dreyfuss, G. (2001). SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. /C^//7:1111-1117. 71. , King, R. , Swanson, M. , Weinstein, E. , and Bedford, M. T. (2004). Small molecule regulators of protein arginine methyltransferases.
Protein Methyltransferases by Fuyuhiko Tamanoi, Steven G. Clarke
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