Arginylation regulates purine nucleotide biosynthesis by enhancing the activity of phosphoribosyl pyrophosphate synthase

Nature Communications

Volumn 6, Issue , 2015, Pages

  Zhang, Fangliang ^a,b   Patel, Devang M ^b   Colavita, Kristen ^a   Rodionova, Irina ^c   Buckley, Brian ^d   Scott, David A ^c   Kumar, Akhilesh ^b   Shabalina, Svetlana A ^e   Saha, Sougata ^a,f   Chernov, Mikhail ^d   Osterman, Andrei L ^c   Kashina, Anna ^a  

^a UNIVERSITY OF PENNSYLVANIA SCHOOL OF VETERINARY MEDICINE   (United States)

^b UNIVERSITY OF MIAMI   (United States)

^c BURNHAM INSTITUTE   (United States)

^d ROSWELL PARK CANCER INSTITUTE   (United States)

^e NATIONAL INSTITUTES OF HEALTH   (United States)

^f TEZPUR UNIVERSITY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCINE; MESSENGER RNA; PHOSPHORIBOSYL PYROPHOSPHATE SYNTHASE; PHOSPHORIBOSYL PYROPHOSPHATE SYNTHASE 1; PHOSPHORIBOSYL PYROPHOSPHATE SYNTHASE 2; PURINE NUCLEOTIDE; SERINE; SYNTHETASE; UNCLASSIFIED DRUG; AMINOACYLTRANSFERASE; ARGININE; ARGINYLTRANSFERASE; LYSINE; PRPS1 PROTEIN, MOUSE; PRPS2 PROTEIN, MOUSE; RIBOSEPHOSPHATE PYROPHOSPHOKINASE;

AMINO ACID; BIOACTIVITY; CELLS AND CELL COMPONENTS; ENZYME ACTIVITY; GENE EXPRESSION; METABOLISM; PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOSYNTHESIS; ENZYME ACTIVITY; ENZYME STABILITY; IN VIVO STUDY; PROTEIN ARGINYLATION; PROTEIN DEGRADATION; PROTEIN PROCESSING; ANIMAL; CELL LINE; CHEMICAL STRUCTURE; GENETICS; HEK293 CELL LINE; HUMAN; KNOCKOUT MOUSE; METABOLISM; MOUSE; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; UBIQUITINATION; WESTERN BLOTTING;

AMINOACYLTRANSFERASES; ANIMALS; ARGININE; BLOTTING, WESTERN; CELL LINE; GLYCINE; HEK293 CELLS; HUMANS; LYSINE; MICE; MICE, KNOCKOUT; MOLECULAR STRUCTURE; PROTEIN PROCESSING, POST-TRANSLATIONAL; PURINE NUCLEOTIDES; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE; RNA, MESSENGER; SERINE; UBIQUITINATION;

EID: 84954443448     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8517     Document Type: Article

References (26)

1. Balzi, E., Choder, M., Chen, W. N., Varshavsky, A. & Goffeau, A. Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae. J. Biol. Chem. 265, 7464-7471 (1990).
2. Kwon, Y. T. et al. An essential role of N-terminal arginylation in cardiovascular development. Science 297, 96-99 (2002).
3. Wong, C. C. L. et al. Global analysis of posttranslational protein arginylation. PLoS Biol. 5, e258 (2007).
4. Saha, S. & Kashina, A. Posttranslational arginylation as a global biological regulator. Dev. Biol. 358, 1-8 (2011).
5. Karakozova, M. et al. Arginylation of beta-actin regulates actin cytoskeleton and cell motility. Science 313, 192-196 (2006).
6. Kurosaka, S. et al. Arginylation-dependent neural crest cell migration is essential for mouse development. PLoS. Genet. 6, e1000878 (2010).
7. Kurosaka, S. et al. Arginylation regulates myofibrils to maintain heart function and prevent dilated cardiomyopathy. J. Mol. Cell. Cardiol. 53, 333-341 (2012).
8. Saha, S. et al. Arginylation and methylation double up to regulate nuclear proteins and nuclear architecture in vivo. Chem. Biol. 18, 1369-1378 (2011).
9. Zhang, F., Saha, S., Shabalina, S. A. & Kashina, A. Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation. Science 329, 1534-1537 (2010).
10. Becker, M. A. et al. Cloning of cDNAs for human phosphoribosylpyrophosphate synthetases 1 and 2 and X chromosome localization of PRPS1 and PRPS2 genes. Genomics 8, 555-561 (1990).
11. Taira, M., Iizasa, T., Yamada, K., Shimada, H. & Tatibana, M. Tissuedifferential expression of two distinct genes for phosphoribosyl pyrophosphate synthetase and existence of the testis-specific transcript. Biochim. Biophys. Acta 1007, 203-208 (1989).
12. Cunningham, J. T., Moreno, M. V., Lodi, A., Ronen, S. M. & Ruggero, D. Protein and nucleotide biosynthesis are coupled by a single rate-limiting enzyme, PRPS2, to drive cancer. Cell 157, 1088-1103 (2014).
13. Tedeschi, P. M. et al. Contribution of serine, folate and glycine metabolism to the ATP, NADPH and purine requirements of cancer cells. Cell Death Dis. 4, e877 (2013).
14. Kastanos, E. K., Woldman, Y. Y. & Appling, D. R. Role of mitochondrial and cytoplasmic serine hydroxymethyltransferase isozymes in de novo purine synthesis in Saccharomyces cerevisiae. Biochemistry 36, 14956-14964 (1997).
15. Scott, D. A. et al. Comparative metabolic flux profiling of melanoma cell lines: beyond the Warburg effect. J. Biol. Chem. 286, 42626-42634 (2011).
16. Aquilonius, S. M. et al. A pharmacokinetic study of neostigmine in man using gas chromatography-mass spectrometry. Eur. J. Clin. Pharmacol. 15, 367-371 (1979).
17. Wong, C. C. et al. Global analysis of posttranslational protein arginylation. PLoS Biol. 5, e258 (2007).
18. Micheli, V., Rocchigiani, M. & Pompucci, G. An HPLC-linked assay of phosphoribosylpyrophosphate synthetase activity in the erythrocytes of adults and children with neurological disorders. Clin. Chim. Acta 227, 79-86 (1994).
19. Zhang, F., Saha, S. & Kashina, A. Arginylation-dependent regulation of a proteolytic product of talin is essential for cell-cell adhesion. J. Cell. Biol. 197, 819-836 (2012).
20. Kudla, G., Murray, A. W., Tollervey, D. & Plotkin, J. B. Coding-sequence determinants of gene expression in Escherichia coli. Science 324, 255-258 (2009).
21. Shabalina, S. A., Spiridonov, N. A. & Kashina, A. Sounds of silence: synonymous nucleotides as a key to biological regulation and complexity. Nucleic Acids Res. 41, 2073-2094 (2013).
22. Ogurtsov, A. Y., Shabalina, S. A., Kondrashov, A. S. & Roytberg, M. A. Analysis of internal loops within the RNA secondary structure in almost quadratic time. Bioinformatics 22, 1317-1324 (2006).
23. Zuker, M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31, 3406-3415 (2003).
24. Mathews, D. H., Turner, D. H. & Zuker, M. RNA secondary structure prediction. Curr. Protoc. Nucleic Acid Chem. 28, 11. 2. 1-11. 2. 17 (2007).
25. Bunk, B. et al. MetaQuant: a tool for the automatic quantification of GC/MSbased metabolome data. Bioinformatics 22, 2962-2965 (2006).
26. Sorci, L. et al. Nicotinamide mononucleotide synthetase is the key enzyme for an alternative route of NAD biosynthesis in Francisella tularensis. Proc. Natl Acad. Sci. USA 106, 3083-3088 (2009).