Recruitment of enzymes as lens structural proteins - PubMed (original) (raw)
Recruitment of enzymes as lens structural proteins
G Wistow et al. Science. 1987.
Abstract
Crystallins, the principal components of the lens, have been regarded simply as soluble, structural proteins. It now appears that the major taxon-specific crystallins of vertebrates and invertebrates are either enzymes or closely related to enzymes. In terms of sequence similarity, size, and other physical characteristics delta-crystallin is closely related to argininosuccinate lyase, tau-crystallin to enolase, and SIII-crystallin to glutathione S-transferase; moreover, it has recently been demonstrated that epsilon-crystallin is an active lactate dehydrogenase. Enzymes may have been recruited several times as lens proteins, perhaps because of the developmental history of the tissue or simply because of evolutionary pragmatism (the selection of existing stable structures for a new structural role).
Similar articles
- Lens crystallins of invertebrates--diversity and recruitment from detoxification enzymes and novel proteins.
Tomarev SI, Piatigorsky J. Tomarev SI, et al. Eur J Biochem. 1996 Feb 1;235(3):449-65. doi: 10.1111/j.1432-1033.1996.00449.x. Eur J Biochem. 1996. PMID: 8654388 Review. - Crystallin genes: specialization by changes in gene regulation may precede gene duplication.
Piatigorsky J. Piatigorsky J. J Struct Funct Genomics. 2003;3(1-4):131-7. J Struct Funct Genomics. 2003. PMID: 12836692 Review. - Recruitment of enzymes and stress proteins as lens crystallins.
Piatigorsky J, Kantorow M, Gopal-Srivastava R, Tomarev SI. Piatigorsky J, et al. EXS. 1994;71:241-50. doi: 10.1007/978-3-0348-7330-7_24. EXS. 1994. PMID: 8032155 Review. - Crystallins of the octopus lens. Recruitment from detoxification enzymes.
Tomarev SI, Zinovieva RD, Piatigorsky J. Tomarev SI, et al. J Biol Chem. 1991 Dec 15;266(35):24226-31. J Biol Chem. 1991. PMID: 1721068 - Evidence for neutral and selective processes in the recruitment of enzyme-crystallins in avian lenses.
Wistow G, Anderson A, Piatigorsky J. Wistow G, et al. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6277-80. doi: 10.1073/pnas.87.16.6277. Proc Natl Acad Sci U S A. 1990. PMID: 2385592 Free PMC article.
Cited by
- Structural Insights into the Interactions of Candidal Enolase with Human Vitronectin, Fibronectin and Plasminogen.
Satala D, Satala G, Karkowska-Kuleta J, Bukowski M, Kluza A, Rapala-Kozik M, Kozik A. Satala D, et al. Int J Mol Sci. 2020 Oct 22;21(21):7843. doi: 10.3390/ijms21217843. Int J Mol Sci. 2020. PMID: 33105833 Free PMC article. - Mass spectrometry-based characterization of the vitreous phosphoproteome.
Tamburro D, Facchiano F, Petricoin EF, Liotta LA, Zhou W. Tamburro D, et al. Proteomics Clin Appl. 2010 Nov;4(10-11):839-46. doi: 10.1002/prca.201000032. Epub 2010 Oct 4. Proteomics Clin Appl. 2010. PMID: 21137027 Free PMC article. - MoonProt 3.0: an update of the moonlighting proteins database.
Chen C, Liu H, Zabad S, Rivera N, Rowin E, Hassan M, Gomez De Jesus SM, Llinás Santos PS, Kravchenko K, Mikhova M, Ketterer S, Shen A, Shen S, Navas E, Horan B, Raudsepp J, Jeffery C. Chen C, et al. Nucleic Acids Res. 2021 Jan 8;49(D1):D368-D372. doi: 10.1093/nar/gkaa1101. Nucleic Acids Res. 2021. PMID: 33245761 Free PMC article. - Optimizing therapy for argininosuccinic aciduria.
Nagamani SC, Lee B, Erez A. Nagamani SC, et al. Mol Genet Metab. 2012 Sep;107(1-2):10-4. doi: 10.1016/j.ymgme.2012.07.009. Epub 2012 Jul 20. Mol Genet Metab. 2012. PMID: 22841516 Free PMC article. Review. - Ultraviolet radiation and the eye: an epidemiologic study.
Taylor HR. Taylor HR. Trans Am Ophthalmol Soc. 1989;87:802-53. Trans Am Ophthalmol Soc. 1989. PMID: 2562534 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases