Human thioesterase superfamily member 2 (hTHEM2) is co-localized with β-tubulin onto the microtubule

Biochemical and Biophysical Research Communications

Volumn 350, Issue 4, 2006, Pages 850-853

  Cheng, Zhongjun ^a,b   Bao, Shilai ^c   Shan, Xiaoyue ^b   Xu, Hang ^b   Gong, Weimin ^a,b  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b INSTITUTE OF BIOPHYSICS   (China)

^c INSTITUTE OF GENETICS AND DEVELOPMENTAL BIOLOGY   (China)

Author keywords

Cellular localization; Hotdog fold; hTHEM2; Microtubule binding; PaaI; siRNA; Thioesterase

Indexed keywords

BETA TUBULIN; GREEN FLUORESCENT PROTEIN; HUMAN THIOESTERASE SUPERFAMILY MEMBER 2; PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; BRAIN; CELL LINE; CELL PROLIFERATION; CONTROLLED STUDY; GENE SILENCING; IMMUNOHISTOCHEMISTRY; KIDNEY; LARGE INTESTINE; LIVER; MICROTUBULE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; SMALL INTESTINE; TISSUE SPECIFICITY;

ANIMALS; HUMANS; MICE; MICROTUBULES; ORGAN SPECIFICITY; THIOLESTER HYDROLASES; TISSUE DISTRIBUTION; TUBULIN;

EID: 33750038561     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.105     Document Type: Article

References (23)

1. Chang K.H., Liang P.H., Beck W., Scholten J.D., and Dunaway-Mariano D. Isolation and characterization of the three polypeptide components of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3. Biochemistry 31 (1992) 5605-5610
2. Hunt M.C., and Alexson S.E. The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog. Lipid Res. 41 (2002) 99-130
3. Duncan J.A., and Gilman A.G. A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS). J. Biol. Chem. 273 (1998) 15830-15837
4. Katz L., and Donadio S. Polyketide synthesis: prospects for hybrid antibiotics. Annu. Rev. Microbiol. 47 (1993) 875-912
5. Smith S. The animal fatty acid synthase: one gene, one polypeptide, seven enzymes. FASEB J. 8 (1994) 1248-1259
6. Trauger J.W., Kohli R.M., Mootz H.D., Marahiel M.A., and Walsh C.T. Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase. Nature 407 (2000) 215-218
7. Scholten J.D., Chang K.H., Babbitt P.C., Charest H., Sylvestre M., and Dunaway-Mariano D. Novel enzymic hydrolytic dehalogenation of a chlorinated aromatic. Science 253 (1991) 182-185
8. Gescher J., Zaar A., Mohamed M., Schagger H., and Fuchs G. Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii. J. Bacteriol. 184 (2002) 6301-6315
9. Olivera E.R., Minambres B., Garcia B., Muniz C., Moreno M.A., Ferrandez A., Diaz E., Garcia J.L., and Luengo J.M. Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: the phenylacetyl-CoA catabolon. Proc. Natl. Acad. Sci. USA 95 (1998) 6419-6424
10. Camp L.A., and Hofmann S.L. Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras. J. Biol. Chem. 268 (1993) 22566-22574
11. Lu J.Y., Verkruyse L.A., and Hofmann S.L. Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. Proc. Natl. Acad. Sci. USA 93 (1996) 10046-10050
12. Hertz R., Magenheim J., Berman I., and Bar-Tana J. Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4alpha. Nature 392 (1998) 512-516
13. Nardini M., and Dijkstra B.W. Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 9 (1999) 732-737
14. Schrag J.D., and Cygler M. Lipases and alpha/beta hydrolase fold. Methods Enzymol. 284 (1997) 85-107
15. Bellizzi III J.J., Widom J., Kemp C., Lu J.Y., Das A.K., Hofmann S.L., and Clardy J. The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis. Proc. Natl. Acad. Sci. USA 97 (2000) 4573-4578
16. Dillon S.C., and Bateman A. The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. BMC Bioinformatics 5 (2004) 109
17. Leesong M., Henderson B.S., Gillig J.R., Schwab J.M., and Smith J.L. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4 (1996) 253-264
18. Cheng Z., Song F., Shan X., Wei Z., Wang Y., Dunaway-Mariano D., and Gong W. Crystal structure of human thioesterase superfamily member 2. Biochem. Biophys. Res. Commun. 349 (2006) 172-177
19. Song F., Zhuang Z., Finci L., Dunaway-Mariano D., Kniewel R., Buglino J.A., Solorzano V., Wu J., and Lima C.D. Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI. J. Biol. Chem. 281 (2006) 11028-11038
20. Kunishima N., Asada Y., Sugahara M., Ishijima J., Nodake Y., Sugahara M., Miyano M., Kuramitsu S., Yokoyama S., and Sugahara M. A novel induced-fit reaction mechanism of asymmetric hot dog thioesterase PAAI. J. Mol. Biol. 352 (2005) 212-228
21. Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M., Garcia J.L., and Diaz E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J. Biol. Chem. 273 (1998) 25974-25986
22. Bao S., Lu T., Wang X., Zheng H., Wang L.E., Wei Q., Hittelman W.N., and Li L. Disruption of the Rad9/Rad1/Hus1 (9-1-1) complex leads to checkpoint signaling and replication defects. Oncogene 23 (2004) 5586-5593
23. Watanabe H., Shiratori T., Shoji H., Miyatake S., Okazaki Y., Ikuta K., Sato T., and Saito T. A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem. Biophys. Res. Commun. 238 (1997) 234-239