• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of pnasPNASInfo for AuthorsSubscriptionsAboutThis Article
Proc Natl Acad Sci U S A. Aug 1990; 87(16): 6277–6280.
PMCID: PMC54516

Evidence for neutral and selective processes in the recruitment of enzyme-crystallins in avian lenses.

Abstract

In apparent contrast to most other tissues, the ocular lenses in vertebrates show striking differences in protein composition between taxa, most notably in the recruitment of different enzymes as major structural proteins. This variability appears to be the result of at least partially neutral evolutionary processes, although there is also evidence for selective modification in molecular structure. Here we describe a bird, the chimney swift (Chaetura pelagica), that lacks delta-crystallin/argininosuccinate lyase, usually the major crystallin of avian lenses. Clearly, delta-crystallin is not specifically required for a functionally effective avian lens. Furthermore the lens composition of the swift is more similar to that of the related hummingbirds than to that of the barn swallow (Hirundo rustica), suggesting that phylogeny is more important than environmental selection in the recruitment of crystallins. However differences in epsilon-crystallin/lactate dehydrogenase-B sequence between swift and hummingbird and other avian and reptilian species suggest that selective pressures may also be working at the molecular level. These differences also confirm the close relationship between swifts and hummingbirds.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (951K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Wistow GJ, Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem. 1988;57:479–504. [PubMed]
  • Piatigorsky J, Wistow GJ. Enzyme/crystallins: gene sharing as an evolutionary strategy. Cell. 1989 Apr 21;57(2):197–199. [PubMed]
  • Wistow G, Piatigorsky J. Recruitment of enzymes as lens structural proteins. Science. 1987 Jun 19;236(4808):1554–1556. [PubMed]
  • Piatigorsky J, Norman B, Jones RE. Conservation of delta-crystallin gene structure between ducks and chickens. J Mol Evol. 1987;25(4):308–317. [PubMed]
  • Piatigorsky J. Delta crystallins and their nucleic acids. Mol Cell Biochem. 1984;59(1-2):33–56. [PubMed]
  • Wawrousek EF, Nickerson JM, Piatigorsky J. Two delta-crystallin polypeptides are derived from a cloned delta 1-crystallin cDNA. FEBS Lett. 1986 Sep 15;205(2):235–240. [PubMed]
  • Wistow GJ, Mulders JW, de Jong WW. The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses. Nature. 1987 Apr 9;326(6113):622–624. [PubMed]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed]
  • Wistow GJ, Lietman T, Williams LA, Stapel SO, de Jong WW, Horwitz J, Piatigorsky J. Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein. J Cell Biol. 1988 Dec;107(6 Pt 2):2729–2736. [PMC free article] [PubMed]
  • Milstone LM, Piatigorsky J. Rates of protein synthesis in explanted embryonic chick lens epithelia: differential stimulation of delta-crystallin synthesis. Dev Biol. 1975 Mar;43(1):91–100. [PubMed]
  • Stapel SO, de Jong WW. Lamprey 48-kDa lens protein represents a novel class of crystallins. FEBS Lett. 1983 Oct 17;162(2):305–309. [PubMed]
  • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. [PMC free article] [PubMed]
  • Hendriks W, Mulders JW, Bibby MA, Slingsby C, Bloemendal H, de Jong WW. Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7114–7118. [PMC free article] [PubMed]
  • Kiltz HH, Keil W, Griesbach M, Petry K, Meyer H. The primary structure of porcine lactate dehydrogenase: isoenzymes M4 and H4. Hoppe Seylers Z Physiol Chem. 1977 Jan;358(1):123–127. [PubMed]
  • Hejtmancik JF, Thompson MA, Wistow G, Piatigorsky J. cDNA and deduced protein sequence for the beta B1-crystallin polypeptide of the chicken lens. Conservation of the PAPA sequence. J Biol Chem. 1986 Jan 15;261(2):982–987. [PubMed]
  • Piatigorsky J, O'Brien WE, Norman BL, Kalumuck K, Wistow GJ, Borras T, Nickerson JM, Wawrousek EF. Gene sharing by delta-crystallin and argininosuccinate lyase. Proc Natl Acad Sci U S A. 1988 May;85(10):3479–3483. [PMC free article] [PubMed]
  • Stapel SO, Zweers A, Dodemont HJ, Kan JH, de Jong WW. epsilon-Crystallin, a novel avian and reptilian eye lens protein. Eur J Biochem. 1985 Feb 15;147(1):129–136. [PubMed]
  • Wistow G, Turnell B, Summers L, Slingsby C, Moss D, Miller L, Lindley P, Blundell T. X-ray analysis of the eye lens protein gamma-II crystallin at 1.9 A resolution. J Mol Biol. 1983 Oct 15;170(1):175–202. [PubMed]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

Formats:

Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...

Links

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...