Functional characterization of Arabidopsis thaliana transthyretin-like protein

BMC Plant Biology

Volumn 10, Issue , 2010, Pages

  Pessoa, João ^a   Sárkány, Zsuzsa ^a   Ferreira da Silva, Frederico ^a   Martins, Sónia ^a   Almeida, Maria R ^a,b   Li, Jianming ^c   Damas, Ana M ^a,b  

^a UNIVERSITY OF PORTO   (Portugal)

^b UNIVERSITY OF PORTO   (Portugal)

^c UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

MEMBRANE PROTEIN; TTL PROTEIN, ARABIDOPSIS;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ARABIDOPSIS; CLONING, MOLECULAR; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 77949472438     PISSN: None     EISSN: 14712229     Source Type: Journal    
DOI: 10.1186/1471-2229-10-30     Document Type: Article

References (24)

1. Nam KE, Li J. The Arabidopsis transthyretin-like protein is a potential substrate of Brassinosteroid Insensitive 1. The Plant Cell 2004, 16:2406-2417. 10.1105/tpc.104.023903, 520942, 15319482.
2. Hennebry SC, Wright HM, Likic VA, Richardson SJ. Structural and functional evolution of transthyretin and transthyretin-like proteins. Proteins: Struct Func Bioinfo 2006, 64:1024-1045.
3. Power DM, Elias NP, Richardson SJ, Mendes J, Soares CM, Santos CRA. Evolution of the thyroid hormone-binding protein, transthyretin. Gen Comp Endocrinol 2000, 119:241-255. 10.1006/gcen.2000.7520, 11017772.
4. Blake CC, Geisow MJ, Oatley SJ, Rérat B, Rérat C. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J Mol Biol 1978, 121:339-356. 10.1016/0022-2836(78)90368-6, 671542.
5. Wojtczak A, Cody V, Luft JR, Pangborn W. Structures of human transthyretin complexed with thyroxine at 2.0 Å resolution and 3',5'-dinitro-N-acetyl-L-thyroxine at 2.2 Å resolution. Acta Crystallogr 1996, D52:758-765.
6. Eneqvist T, Lundberg E, Nilsson L, Abagyan R, Sauer-Eriksson AE. The transthyretin-related protein family. Eur J Biochem 2003, 270:518-532. 10.1046/j.1432-1033.2003.03408.x, 12542701.
7. Hennebry SC. Evolutionary changes to transthyretin: structure and function of a transthyretin-like ancestral protein. FEBS J 2009, 276:5367-5379. 10.1111/j.1742-4658.2009.07246.x, 19725880.
8. Reumann S, Babujee L, Ma C, Wienkoop S, Siemsen T, Antonicelli GE, Rasche N, Lüder F, Weckwerth W, Jahn O. Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways, and defense mechanisms. The Plant Cell 2007, 19:3170-3193. 10.1105/tpc.107.050989, 2174697, 17951448.
9. Ramazzina I, Folli C, Secchi A, Berni R, Percudani R. Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. Nat Chem Biol 2006, 2:144-148. 10.1038/nchembio768, 16462750.
10. Hennebry SC, Law RHP, Richardson SJ, Buckle AM, Whisstock JC. The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase. J Mol Biol 2006, 359:1389-1399. 10.1016/j.jmb.2006.04.057, 16787778.
11. Lundberg E, Backstrom S, Sauer UH, Sauer Eriksson AE. The transthyretin-related protein: Structural investigation of a novel protein family. J Struct Biol 2006, 155:445-457. 10.1016/j.jsb.2006.04.002, 16723258.
12. Zanotti G, Cendron L, Ramazzina I, Folli C, Percudani R, Berni R. Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter. J Mol Biol 2006, 363:1-9. 10.1016/j.jmb.2006.07.079, 16952372.
13. Jung D-K, Lee Y, Park SG, Park BC, Kim G-H, Rhee D. Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family. Proc Nat Acad Sci USA 2006, 103:9790-9795. 10.1073/pnas.0600523103, 1502532, 16782815.
14. Lee Y, Lee DH, Kho CW, Lee AY, Jang M, Cho S, Lee CH, Lee JS, Myung PK, Park BC, Park SG. Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. FEBS Lett 2005, 579:4769-4774. 10.1016/j.febslet.2005.07.056, 16098976.
15. Siegel L, Monty K. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases. Biochim Biophys Acta 1966, 112:346-362. 10.1016/0926-6585(66)90333-5, 5329026.
16. Lee Y, Park BC, Lee DH, Bae K-H, Cho S, Lee CH, Lee JS, Myung PK, Park SG. Mouse transthyretin-related protein is a hydrolase which degrades 5-hydroxyisourate, the end product of the uricase reaction. Mol Cells 2006, 22:141-145.
17. Kahn K, Tipton PA. Spectroscopic characterization of intermediates in the urate oxidase reaction. Biochemistry 1998, 37:11651-11659. 10.1021/bi980446g, 9709003.
18. Kim K, Park J, Rhee S. Structural and functional basis for (S)-allantoin formation in the ureide pathway. J Biol Chem 2007, 282:23457-23464. 10.1074/jbc.M703211200, 17567580.
19. Cendron L, Berni R, Folli C, Ramazzina I, Percudani R, Zanotti G. The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides Insights into the mechanism of uric acid degradation. J Biol Chem 2007, 282:18182-18189. 10.1074/jbc.M701297200, 17428786.
20. Jeffery CJ. Moonlighting proteins. Trends Biochem Sci 1999, 24:8-11. 10.1016/S0968-0004(98)01335-8, 10087914.
21. Jeffery CJ. Moonlighting proteins: old proteins learning new tricks. Trends Genetics 2003, 19:415-417.
22. Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Prot Science 1995, 4:2411-2423.
23. Almeida MR, Damas AM, Lans MC, Brouwer A, Saraiva MJ. Thyroxine binding to transthyretin Met 119. Comparative studies of different heterozygotic carriers and structural analysis. Endocrine 1997, 6:309-315. 10.1007/BF02820508, 9368688.
24. Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 22:4673-4680. 10.1093/nar/22.22.4673, 308517, 7984417.