Home LiteratureArticle Details
PMID: 3174623 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 85 ·No. 19 ·1988-10-00 ·Pages 7114-8

Hendriks W, Mulders JW, Bibby MA, Slingsby C, Bloemendal H, de Jong WW

Abstract

To investigate whether or not duck lens epsilon-crystallin and duck heart lactate dehydrogenase (LDH) B4 are the product of the same gene, we have isolated and sequenced cDNA clones of duck epsilon-crystallin. By using these clones we demonstrate that there is a single-copy Ldh-B gene in duck and in chicken. In the duck lens this gene is overexpressed, and its product is subject to posttranslational modification. Reconstruction of the evolutionary history of the LDH protein family reveals that the mammalian Ldh-C gene most probably originated from an ancestral Ldh-A gene and that the amino acid replacement rate in LDH-C is approximately 4 times the rate in LDH-A. Molecular modeling of LDH-B sequences shows that the increased thermostability of the avian tetramer might be explained by mutations that increase the number of ion pairs. Furthermore, the replacement of bulky side chains by glycines on the corners of the duck protein suggests an adaptation to facilitate close packing in the lens.

MeSH Terms
Animals Base Sequence Chickens Crystallins/genetics DNA/analysis Ducks Isoenzymes L-Lactate Dehydrogenase/genetics Molecular Sequence Data Phylogeny
Chemicals
Crystallins Isoenzymes DNA L-Lactate Dehydrogenase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hendriks W
Department of Biochemistry, University of Nijmegen, The Netherlands.
Mulders J W
Bibby M A
Slingsby C
Bloemendal H
de Jong W W
References (42)
42 references, click to expand
  1. The interpretation of protein structures: estimation of static accessibility.
    J Mol Biol. 1971 Feb 14;55(3):379-400 PMID: 5551392
  2. EVOLUTION OF LACTIC DEHYDROGENASES.
    Fed Proc. 1964 Nov-Dec;23:1258-66 PMID: 14236134
  3. The primary structure of porcine lactate dehydrogenase: isoenzymes M4 and H4.
    Hoppe Seylers Z Physiol Chem. 1977 Jan;358(1):123-7 PMID: 838465
  4. Structural adaptations of lactate dehydrogenase isozymes.
    Proc Natl Acad Sci U S A. 1977 Jul;74(7):2677-81 PMID: 197516
  5. Sequence data handling by computer.
    Nucleic Acids Res. 1977 Nov;4(11):4037-51 PMID: 593900
  6. Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA.
    Eur J Biochem. 1980 Jun;107(2):303-14 PMID: 6772444
  7. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing.
    J Mol Biol. 1980 Oct 25;143(2):161-78 PMID: 6260957
  8. Primary structure of the bovine beta-crystallin Bp chain. Internal duplication and homology with gamma-crystallin.
    Eur J Biochem. 1981 Dec;121(1):83-91 PMID: 7035168
  9. Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 A resolution.
    J Mol Biol. 1981 Sep 15;151(2):289-307 PMID: 7338899
  10. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.
    Proc Natl Acad Sci U S A. 1982 Apr;79(7):2360-4 PMID: 6285380
  11. Short-range order of crystallin proteins accounts for eye lens transparency.
    Nature. 1983 Mar 31-Apr 6;302(5907):415-7 PMID: 6835373
  12. Amino acid sequence studies on lactate dehydrogenase C4 isozymes from mouse and rat testes.
    J Biol Chem. 1983 Jun 10;258(11):7005-16 PMID: 6343385
  13. Evolutionary relationships of vertebrate lactate dehydrogenase isozymes A4 (muscle), B4 (heart), and C4 (testis).
    J Biol Chem. 1983 Jun 10;258(11):7029-32 PMID: 6853510
  14. Ion-pairs in proteins.
    J Mol Biol. 1983 Aug 25;168(4):867-85 PMID: 6887253
  15. Genomic sequencing.
    Proc Natl Acad Sci U S A. 1984 Apr;81(7):1991-5 PMID: 6326095
  16. Lactate dehydrogenase. Biochemistry and function of lactate dehydrogenase.
    Cell Biochem Funct. 1984 Jul;2(3):131-4 PMID: 6383647
  17. Genetic, developmental and evolutionary aspects of the lactate dehydrogenase isozyme system.
    Cell Biochem Funct. 1984 Jul;2(3):134-9 PMID: 6383648
  18. epsilon-Crystallin, a novel avian and reptilian eye lens protein.
    Eur J Biochem. 1985 Feb 15;147(1):129-36 PMID: 3971972
  19. Protein structure and gene organization of mouse lactate dehydrogenase-A isozyme.
    Eur J Biochem. 1985 Jun 3;149(2):215-25 PMID: 3996406
  20. Epidermal growth factor or serum stimulation of rat fibroblasts induces an elevation in mRNA levels for lactate dehydrogenase and other glycolytic enzymes.
    Nucleic Acids Res. 1985 Feb 11;13(3):711-26 PMID: 3873645
  21. Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens beta gamma-crystallins.
    Nature. 1985 Jun 27-Jul 3;315(6022):771-3 PMID: 3925350
  22. Highly conserved sequences in the 3' untranslated region of mRNAs coding for homologous proteins in distantly related species.
    Nucleic Acids Res. 1985 May 24;13(10):3723-37 PMID: 4011440
  23. An improved DNA sequencing strategy.
    Anal Biochem. 1985 May 15;147(1):114-9 PMID: 2992313
  24. Complete structure of the hamster alpha A crystallin gene. Reflection of an evolutionary history by means of exon shuffling.
    J Mol Biol. 1985 Sep 20;185(2):273-84 PMID: 4057247
  25. Genomic organization of human lactate dehydrogenase-A gene.
    Biochem J. 1985 Nov 1;231(3):537-41 PMID: 3000353
  26. Interaction of bovine heart lactate dehydrogenase with erythrocyte lipids.
    Biochim Biophys Acta. 1986 Feb 13;855(1):99-104 PMID: 3942747
  27. Sequence and expression of a major egg antigen from Schistosoma mansoni. Homologies to heat shock proteins and alpha-crystallins.
    Mol Biochem Parasitol. 1986 Nov;21(2):179-88 PMID: 3097539
  28. Centrosomal proteins and lactate dehydrogenase possess a common epitope in human cell lines.
    Proc Natl Acad Sci U S A. 1987 Feb;84(4):1000-4 PMID: 2434947
  29. The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses.
    Nature. 1987 Apr 9-15;326(6113):622-4 PMID: 3561501
  30. Recruitment of enzymes as lens structural proteins.
    Science. 1987 Jun 19;236(4808):1554-6 PMID: 3589669
  31. Molecular cloning and nucleotide sequence of the cDNA for sperm-specific lactate dehydrogenase-C from mouse.
    Biochem J. 1987 Mar 1;242(2):619-22 PMID: 2439071
  32. Epitopes of human testis-specific lactate dehydrogenase deduced from a cDNA sequence.
    Proc Natl Acad Sci U S A. 1987 Aug;84(15):5311-5 PMID: 2440048
  33. Aldose reductase and p-crystallin belong to the same protein superfamily as aldehyde reductase.
    FEBS Lett. 1987 Aug 10;220(1):209-13 PMID: 3111886
  34. Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.
    Nature. 1987 Nov 5-11;330(6143):41-6 PMID: 3118211
  35. Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog.
    Proc Natl Acad Sci U S A. 1988 Jan;85(1):11-5 PMID: 2829166
  36. The cDNA and protein sequences of human lactate dehydrogenase B.
    Biochem J. 1987 Dec 15;248(3):933-6 PMID: 3435492
  37. Evolutionary and functional relationships between the basic and acidic beta-crystallins.
    Exp Eye Res. 1988 Mar;46(3):375-403 PMID: 3350075
  38. Dogfish alpha-crystallin sequences. Comparison with small heat shock proteins and Schistosoma egg antigen.
    J Biol Chem. 1988 Apr 15;263(11):5141-9 PMID: 3356684
  39. Gene sharing by delta-crystallin and argininosuccinate lyase.
    Proc Natl Acad Sci U S A. 1988 May;85(10):3479-83 PMID: 3368457
  40. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue.
    Annu Rev Biochem. 1988;57:479-504 PMID: 3052280
  41. The role of cysteine oxidation in the thermal inactivation of T4 lysozyme.
    Protein Eng. 1987 Feb-Mar;1(2):101-5 PMID: 3507692
  42. Evolution of a gene. Multiple genes for LDH isozymes provide a model of the evolution of gene structure, function and regulation.
    Science. 1975 Jul 11;189(4197):102-14 PMID: 1138367
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.85.19.7114
Published
1988-10-00
Pages
7114-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC282134
Subset
IM
Databases
GENBANK
J03869
External Links
PubMed source DOI: 10.1073/pnas.85.19.7114 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2