Dual activity of certain HIT-proteins: A. thaliana Hint4 and C. elegans DcpS act on adenosine 5′-phosphosulfate as hydrolases (forming AMP) and as phosphorylases (forming ADP)

FEBS Letters

Volumn 584, Issue 1, 2010, Pages 93-98

  Guranowski, Andrzej ^a   Wojdyła, Anna Maria ^a   Zimny, Jarosław ^a   Wypijewska, Anna ^b   Kowalska, Joanna ^b   Jemielity, Jacek ^b   Davis, Richard E ^c   Bieganowski, Paweł ^d  

^a POZNA UNIVERSITY OF LIFE SCIENCES   (Poland)

^b UNIVERSITY OF WARSAW   (Poland)

^c UNIVERSITY OF COLORADO SCHOOL OF MEDICINE   (United States)

^d MOSSAKOWSKI MEDICAL RESEARCH CENTRE   (Poland)

Author keywords

Adenosine 5 phosphosulfate hydrolysis; Adenosine 5 phosphosulfate phosphorolysis; Dual catalytic activity; Histidine triad family protein

Indexed keywords

ADENOSINE 5' PHOSPHOSULFATE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ARABIDOPSIS PROTEIN; CAENORHABDITIS ELEGANS PROTEIN; HISTIDINE; HYDROLASE; PHOSPHATE; PHOSPHORYLASE; PROTEIN DCPS; PROTEIN HINT4; SULFATASE; UNCLASSIFIED DRUG;

ARABIDOPSIS; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROLYSIS; METABOLISM; NONHUMAN; NUCLEOTIDE SEQUENCE; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION;

ADENOSINE DIPHOSPHATE; ADENOSINE MONOPHOSPHATE; ADENOSINE PHOSPHOSULFATE; ANIMALS; ARABIDOPSIS; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; HYDROGEN-ION CONCENTRATION; HYDROLASES; HYDROLYSIS; MULTIENZYME COMPLEXES; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLATION; PYROPHOSPHATASES; SUBSTRATE SPECIFICITY; SULFATASES;

ARABIDOPSIS THALIANA; CAENORHABDITIS ELEGANS;

EID: 71549154052     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.11.003     Document Type: Article

References (19)

1. Barnes L.D., Garrison P.N., Siprashvili Z., Guranowski A., Robinson A.K., Ingram S.W., Croce C.M., Ohta M., and Huebner K. Fhit, a putative tumor suppressor in humans, is a dinucleoside 5′,5‴-P1,P3-triphosphate hydrolase. Biochemistry 35 (1996) 11529-11535
2. Guranowski A., Wojdyła A.M., Pietrowska-Borek M., Bieganowski P., Khurs E.N., Cliff M.J., Blackburn G.M., Błaziak D., and Stec W.J. Fhit proteins can also recognize substrates other than dinucleoside polyphosphates. FEBS Lett. 582 (2008) 3138-3152
3. 2,2,7GpppG decapping: activities in Ascaris embryos and characterization of C. elegans scavenger DcpS. RNA 10 (2004) 1609-1624
4. Bail S., and Kiledjian M. DcpS, a general modulator of cap-binding protein-dependent processes?. RNA Biol. 5 (2008) 1-4
5. Banerjee H., Palenchar J.B., Lukaszewicz M., Bojarska E., Stepinski J., Jemielity J., Guranowski A., Ng S., Wah D., Darzynkiewicz E., and Bellofatto V. Identification of the HIT-45 protein from Trypanosoma brucei as an FHIT protein/dinucleoside triphosphatase: Substrate specificity studies on the recombinant and endogenous proteins. RNA 15 (2009) 1554-1564
6. Carmi-Levy I., Yannay-Cohen N., Kay G., Razin E., and Nechushtan H. Diadenosine tetraphosphate hydrolase is part of the transcriptional regulation network in immunologically activated mast cells. Mol. Cell. Biol. 28 (2008) 5777-5784
7. Kowalska J., Lewdorowicz M., Darzynkiewicz E., and Jemielity J. A simple and rapid synthesis of nucleotide analogues containing a phosphorothioate moiety at the terminal position of the phosphate chain. Tetrahedron Lett. 48 (2007) 5475-5479
8. Guranowski A., Starzyńska E., Günther Sillero M.A., and Sillero A. Conversion of adenosine (5′)oligophospho(5′)adenosines into inosine(5′)oligophospho(5′)inosines by non-specific adenylate deaminase from the snail Helix pomatia. Biochim. Biophys. Acta 1243 (1995) 78-84
9. Bailey-Wood R., Dodgson K.S., and Rose F.A. A rat liver sulphohydrolase enzyme acting on adenylyl sulphate. Biochem. J. 112 (1969) 257-258
10. Brüser T., Selmer T., and Dahl C. "ADP-sulfurylase" from Thiobacillus denitrificans is an adenylylsulfate:phosphate adenylyltransferase and belongs to a new family of nucleotidyltransferases. J. Biol. Chem. 275 (2000) 1691-1698
11. Robbins P.W., and Lipmann F. Separation of the two enzymatic phases in active sulfate synthesis. J. Biol. Chem. 233 (1958) 681-685
12. In: Purich D.L., and Allison R.D. (Eds). The Enzyme Reference: A Comprehensive Guide to Enzyme Nomenclature, Reactions, and Methods (2002), Academic Press, Amsterdam p. 796
13. Schmidt A., and Jäger K. Open questions about sulfur metabolism in plants. Annu. Rev. Plant Physiol., Mol. Biol. 43 (1992) 325-349
14. In: Buchannan B.B., Gruissem W., and Jones R.L. (Eds). Biochemistry and Molecular Biology of Plants (2000), American Society of Plant Physiologists, Rockville, MD pp. 824-825 and 1223-1224
15. Szuwart M., Starzyńska E., Pietrowska-Borek M., and Guranowski A. Calcium-stimulated guanosine-inosine nucleosidase from yellow lupin (Lupinus luteus). Phytochemistry 67 (2006) 1476-1485
16. Bzowska A., Kulikowska E., and Shugar D. Purine nucleoside phosphorylases: properties, functions, and clinical aspects. Pharmacol. Ther. 88 (2000) 349-425
17. Guranowski A. Specific and nonspecific enzymes involved in the catabolism of mononucleoside and dinucleoside polyphosphates. Pharmacol. Ther. 87 (2000) 117-139
18. Guranowski A., and Blanquet S. Diadenosine 5′,5′′′-P1,P4-tetraphosphate α,β-phosphorylase from yeast supports nucleoside diphosphate-phosphate exchange. J. Biol. Chem. 261 (1986) 5943-5946
19. Gu M., Fabrega C., Liu S.W., Liu H., Kiledjian M., and Lima C.D. Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity. Mol. Cell 14 (2004) 67-80