Abstract
Bioinformatics programs are highly accurate in identifying protein families directly from protein sequences, even when the sequence identity is very low. The transthyretin-related proteins (TRPs) are one example of a protein family that has been identified. Whereas transthyretin (TTR) is well-characterized both in vivo and in vitro, only recently has research focused on the TRPs. Their structural similarity to TTR has been verified, and their function as a 5-hydroxyisourate (HIU) hydrolase has been established. In this review we discuss structural aspects of TRP function. We also discuss the still unknown transthyretin-like proteins (TLPs) that are seemingly unique to nematodes.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Cole C, Barber JD, Barton GJ. 2008. The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36:W197–W201.
Colon W, Kelly JW. 1992. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31:8654–8660.
Cusa E, Obradors N, Baldoma L, Badia J, Aguilar J. 1999. Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli. J Bacteriol 181:7479–7484.
Eneqvist T, Lundberg E, Nilsson L, Abagyan R, Sauer-Eriksson AE. 2003. The transthyretin-related protein family. Eur J Biochem 270:518–532.
Fisher SH. 1999. Regulation of nitrogen metabolism in Bacillus subtilis: vive la difference! Mol Microbiol 32:223–232.
Hansen M, Hsu AL, Dillin A, Kenyon C. 2005. New genes tied to endocrine, metabolic, and dietary regulation of lifespan from a Caenorhabditis elegans genomic RNAi screen. PLoS Genet 1:119–128.
Hennebry SC, Law RH, Richardson SJ, Buckle AM, Whisstock JC. 2006a. The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase. J Mol Biol 359:1389–1399.
Hennebry SC, Wright HM, Likic VA, Richardson SJ. 2006b. Structural and functional evolution of transthyretin and transthyretin-like proteins. Proteins 64:1024–1045.
Hornberg A, Eneqvist T, Olofsson A, Lundgren E, Sauer-Eriksson AE. 2000. A comparative analysis of 23 structures of the amyloidogenic protein transthyretin. J Mol Biol 302:649–669.
Jung DK, Lee Y, Park SG, Park BC, Kim GH, Rhee S. 2006. Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family. Proc Natl Acad Sci USA 103:9790–9795.
Kahn K, Tipton PA. 1998. Spectroscopic characterization of intermediates in the urate oxidase reaction. Biochemistry 37:11651–11659.
Kall L, Krogh A, Sonnhammer EL. 2004. A combined transmembrane topology and signal peptide prediction method. J Mol Biol 338:1027–1036.
Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, McWilliam H, Valentin F, Wallace IM, Wilm A, Lopez R, Thompson JD, Gibson TJ, Higgins DG. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2947–2948.
Lee Y, Lee DH, Kho CW, Lee AY, Jang M, Cho S, Lee CH, Lee JS, Myung PK, Park BC, Park SG. 2005. Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. FEBS Lett 579:4769–4774.
Lee Y, Park BC, Lee do H, Bae KH, Cho S, Lee CH, Lee JS, Myung PK, Park SG. 2006. Mouse transthyretin-related protein is a hydrolase which degrades 5-hydroxyisourate, the end product of the uricase reaction. Mol Cells 22:141–145.
Liz MA, Faro CJ, Saraiva MJ, Sousa MM. 2004. Transthyretin, a new cryptic protease. J Biol Chem 279:21431–21438.
Lundberg E, Backstrom S, Sauer UH, Sauer-Eriksson AE. 2009. The transthyretin-related protein: structural investigation of a novel protein family. J Struct Biol 155:445–457.
Lundberg E, Olofsson A, Westermark GT, Sauer-Eriksson AE. 2009. Fibril-formation properties of human and piscine transthyretin, and E. coli transthyretin-related protein. FEBS J 276(7):1999–2011.
Nygaard P. 1983. Utilization of preformed purine bases and nucleosides. In: A. Munch-Petersen (ed.), Metabolism of nucleotides, nucleosides and nucleobases in microorganism. Academic Press, London, UK p. 27–93.
Prapunpoj P, Yamauchi K, Nishiyama N, Richardson SJ, Schreiber G. 2000. Evolution of structure, ontogeny of gene expression, and function of Xenopus laevis transthyretin. Am J Physiol Regul Integr Comp Physiol 279:R2026–R2041.
Ramazzina I, Folli C, Secchi A, Berni R, Percudani R. 2006. Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. Nat Chem Biol 2:144–148.
Santos SD, Costa R, Teixeira PF, Gottesman M, Cardoso I, Saraiva MJ. 2008. Amyloidogenic properties of transthyretin-like protein (TLP) from Escherichia coli. FEBS Lett 582:2893–2898.
Sarma AD, Serfozo P, Kahn K, Tipton PA. 1999. Identification and purification of hydroxyisourate hydrolase, a novel ureide-metabolizing enzyme. J Biol Chem 274:33863–33865.
Schultz AC, Nygaard P, Saxild HH. 2001. Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator. J Bacteriol 183:3293–3302.
Sonnhammer EL, Durbin R. 1997. Analysis of protein domain families in Caenorhabditis elegans. Genomics 46:200–216.
Wojtczak A, Cody V, Luft JR, Pangborn W. 2001. Structure of rat transthyretin (rTTR) complex with thyroxine at 2.5 A resolution: first non-biased insight into thyroxine binding reveals different hormone orientation in two binding sites. Acta Crystallogr D Biol Crystallogr 57:1061–1070.
Xi H, Schneider BL, Reitzer L. 2000. Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage. J Bacteriol 182:5332–5341.
Zanotti G, Cendron L, Ramazzina I, Folli C, Percudani R, Berni R. 2006. Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter. J Mol Biol 363:1–9.
Acknowledgements
The authors thank Uwe H. Sauer and Tobias Hainzl for valuable discussions, and Terese Bergfors for critical reading of the manuscript.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Sauer-Eriksson, A.E., Linusson, A., Lundberg, E. (2009). Transthyretin-Related and Transthyretin-like Proteins. In: Richardson, S.J., Cody, V. (eds) Recent Advances in Transthyretin Evolution, Structure and Biological Functions. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-00646-3_7
Download citation
DOI: https://doi.org/10.1007/978-3-642-00646-3_7
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-00645-6
Online ISBN: 978-3-642-00646-3
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)