NRMT is an α-N-methyltransferase that methylates RCC1 and retinoblastoma protein

Nature

Volumn 466, Issue 7310, 2010, Pages 1125-1128

  Schaner Tooley, Christine E ^a   Petkowski, Janusz J ^a   Muratore Schroeder, Tara L ^b   Balsbaugh, Jeremy L ^b   Shabanowitz, Jeffrey ^b   Sabat, Michal ^b   Minor, Wladek ^a   Hunt, Donald F ^a,b   MacAra, Ian G ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

METHYLTRANSFERASE; N TERMINAL RCC1 METHYLTRANSFERASEN TERMINAL; PROTEIN; RAN GUANINE NUCLEOTIDE EXCHANGE FACTOR; RAN PROTEIN; RETINOBLASTOMA PROTEIN; SET PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID; BACTERIUM; CHROMOSOME; ENZYME ACTIVITY; FUNGUS; METHYLATION; PHENOTYPE; PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHROMOSOME SEGREGATION; CONTROLLED STUDY; FEMALE; GENE INACTIVATION; HUMAN; HUMAN CELL; MITOSIS SPINDLE; MOLECULAR DOCKING; MUTATIONAL ANALYSIS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN METHYLATION; PROTEIN PROCESSING;

CELL CYCLE PROTEINS; CELL LINE; CHROMOSOME SEGREGATION; GENE KNOCKDOWN TECHNIQUES; GUANINE NUCLEOTIDE EXCHANGE FACTORS; HELA CELLS; HISTONE CHAPERONES; HUMANS; METHYLTRANSFERASES; MITOTIC SPINDLE APPARATUS; MODELS, MOLECULAR; MUTATION; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RETINOBLASTOMA PROTEIN; TRANSCRIPTION FACTORS;

ANIMALIA; BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 77956190789     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09343     Document Type: Article

References (32)

1. Brosius, J. & Chen, R. The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes. FEBS Lett. 68, 105-109 (1976).
2. Wittmann-Liebold, B. & Pannenbecker, R. Primary structure of protein L33 from the large subunit of the Escherichia coli ribosome. FEBS Lett. 68, 115-118 (1976).
3. Chen, T. et al. N-terminal a-methylation of RCC1 is necessary for stable chromatin association and normal mitosis. Nature Cell Biol. 9, 596-603 (2007).
4. Meng, F. et al. Molecular-level description of proteins from Saccharomyces cerevisiae using quadrupole FT hybrid mass spectrometry for top down proteomics. Anal. Chem. 76, 2852-2858 (2004).
5. Sadaie, M., Shinmyozu, K. & Nakayama, J. A conserved SET domain methyltransferase, Set11, modifies ribosomal protein Rpl12 in fission yeast. J. Biol. Chem. 283, 7185-7195 (2008).
6. Pettigrew, G. W. & Smith, G. M. Novel N-terminal protein blocking group identified as dimethylproline. Nature 265, 661-662 (1977).
7. Martinage, A., Briand, G., Van Dorsselaer, A., Turner, C. H. & Sautiere, P. Primary structure of histone H2B from gonads of the starfish Asterias rubens. Identification of an N-dimethylproline residue at the amino-terminal. Eur. J. Biochem. 147, 351-359 (1985).
8. Nomoto, M., Hayashi, H. & Iwai, K. Tetrahymena histone H2B. Complete amino acid sequence. J. Biochem. 91, 897-904 (1982).
9. Grimm, R. et al. Postimport methylation of the small subunit of ribulose-1,5-bisphosphate carboxylase in chloroplasts. FEBS Lett. 408, 350-354 (1997).
10. Henry, G. D. et al. The occurrence of a-N-trimethylalanine as the N-terminal amino acid of some myosin light chains. FEBS Lett. 144, 11-15 (1982).
11. Hao, Y. & Macara, I. G. Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1. J. Cell Biol. 182, 827-836 (2008).
12. Stock, A., Clarke, S., Clarke, C. & Stock, J. N-terminal methylation of proteins: structure, function and specificity. FEBS Lett. 220, 8-14 (1987).
13. Bloom, K. S. & Anderson, J. N. Fractionation and characterization of chromosomal proteins by the hydroxyapatite dissociation method. J. Biol. Chem. 253, 4446-4450 (1978).
14. Simon, R. H. & Felsenfeld, G. A new procedure for purifying histone pairs H2A1H2B and H31H4 from chromatin using hydroxylapatite. Nucleic Acids Res. 6, 689-696 (1979).
15. Duncan, E. M. et al. Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation. Cell 135, 284-294 (2008).
16. Hu, R. M. et al. Gene expression profiling in the human hypothalamus-pituitaryadrenal axis and full-length cDNA cloning. Proc. Natl Acad. Sci. USA 97, 9543-9548 (2000).
17. Scheerer, P. et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 455, 497-502 (2008).
18. Yu, W. et al. A novel human BTB-kelch protein KLHL31, strongly expressed in muscle and heart, inhibits transcriptional activities of TRE and SRE. Mol. Cells 26, 443-453 (2008).
19. Yamamoto, H. et al. Paradoxical increase in retinoblastoma protein in colorectal carcinomas may protect cells from apoptosis. Clin. Cancer Res. 5, 1805-1815 (1999).
20. Boyer, S. N., Wazer, D. E. & Band, V. E7 protein of human papilloma virus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome pathway. Cancer Res. 56, 4620-4624 (1996).
21. Dyson, N., Howley, P. M., Munger, K. & Harlow, E. The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product. Science 243, 934-937 (1989).
22. Carroll, A. J., Heazlewood, J. L., Ito, J. & Millar, A. H. Analysis of the Arabidopsis cytosolic ribosome proteome provides detailed insights into its components and their post-translational modification. Mol. Cell. Proteomics 7, 347-369 (2008).
23. Baker, N. A., Sept, D., Joseph, S., Holst, M. J. & McCammon, J. A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).
24. Chen, T., Brownawell, A. M. & Macara, I. G. Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5. Mol. Cell. Biol. 24, 6608-6619 (2004).
25. Dignani, J. D., Lebovitz, R. M. & Roeder, R. G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489 (1983).
26. Schroeder, M. J., Shabanowitz, J., Schwartz, J. C., Hunt, D. F. & Coon, J. J. A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry. Anal. Chem. 76, 3590-3598 (2004).
27. Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858 (1996).
28. Martin, S. E., Shabanowitz, J., Hunt, D. F. & Marto, J. A. Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 72, 4266-4274 (2000).
29. Syka, J. E. et al. Novel linear quadrupole ion trap/FT mass spectrometer: performance characterization and use in the comparative analysis of histone H3 post-translational modifications. J. Proteome Res. 3, 621-626 (2004).
30. Syka, J. E., Coon, J. J., Schroeder, M. J., Shabanowitz, J. & Hunt, D. F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl Acad. Sci. USA 101, 9528-9533 (2004).
31. Udeshi, N. D., Compton, P. D., Shabanowitz, J., Hunt, D. F. & Rose, K. L. Methods for analyzing peptides and proteins on a chromatographic timescale by electrontransfer dissociation mass spectrometry. Nature Protocols 3, 1709-1717 (2008).
32. Abagyan, R., Totrov, M. & Kuznetsov, D. J. ICM-a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J. Comput. Chem. 15, 488-506 (1994).