Home LiteratureArticle Details
PMID: 1528862 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Primary structure of tektin A1: comparison with intermediate-filament proteins and a model for its association with tubulin.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 89 ·No. 18 ·1992-09-15 ·Pages 8567-71

Norrander JM, Amos LA, Linck RW

Abstract

Tektins are proteins that form filamentous polymers in the walls of ciliary and flagellar microtubules and that have biochemical and immunological properties similar to those of intermediate-filament proteins. We report here the sequence of a cDNA for tektin A1, one of the main tektins from Strongylocentrotus purpuratus sea urchin embryos. By hybridization analysis, tektin A mRNA appears maximally at ciliogenesis. The predicted structure of tektin A1 (M(r) 52,955) is a series of alpha-helical rod segments separated by nonhelical linkers. The two halves of the rod appear homologous and are probably related by gene duplication. Comparison of tektin A1 with intermediate-filament proteins, including nuclear lamins, reveals a low amino acid homology but similar molecular motif, i.e., pattern of helical and nonhelical domains. This study indicates that tektins are unique proteins but may be evolutionarily related to intermediate-filament proteins, and suggests a structural basis for the interaction of tektins and tubulin in microtubules.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cloning, Molecular Gene Expression Microtubule Proteins/chemistry,genetics Molecular Sequence Data RNA, Messenger/genetics Sea Urchins/embryology Sequence Alignment Tubulin/metabolism
Chemicals
Microtubule Proteins RNA, Messenger Tubulin tektins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Norrander J M
Department of Cell Biology and Neuroanatomy, University of Minnesota, Minneapolis 55455.
Amos L A
Linck R W
References (33)
33 references, click to expand
  1. Segmented alpha-helical coiled-coil structure of the protein giardin from the Giardia cytoskeleton.
    J Mol Biol. 1988 Dec 5;204(3):789-95 PMID: 3225852
  2. Quantal tektin synthesis and ciliary length in sea-urchin embryos.
    J Cell Sci. 1989 Mar;92 ( Pt 3):403-13 PMID: 2592446
  3. Studies of tektin filaments from flagellar microtubules by immunoelectron microscopy.
    J Cell Sci Suppl. 1986;5:55-68 PMID: 3308918
  4. Production of single-stranded plasmid DNA.
    Methods Enzymol. 1987;153:3-11 PMID: 3323803
  5. Characterization of antibodies as probes for structural and biochemical studies of tektins from ciliary and flagellar microtubules.
    J Cell Sci. 1987 Nov;88 ( Pt 4):453-66 PMID: 3332669
  6. Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences.
    Science. 1988 Jul 22;241(4864):459-62 PMID: 3393912
  7. Biochemical characterization of tektins from sperm flagellar doublet microtubules.
    J Cell Biol. 1987 Apr;104(4):1069-75 PMID: 3558479
  8. Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode.
    EMBO J. 1989 Nov;8(11):3221-7 PMID: 2583097
  9. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.
    J Biol Chem. 1987 Jul 25;262(21):10035-8 PMID: 3611052
  10. X-ray diffraction patterns from microtubules and neurofilaments in axoplasm.
    J Mol Biol. 1987 Sep 20;197(2):205-18 PMID: 3681995
  11. Localization of tektin filaments in microtubules of sea urchin sperm flagella by immunoelectron microscopy.
    J Cell Biol. 1985 Jan;100(1):126-35 PMID: 3880749
  12. Proteins closely similar to flagellar tektins are detected in cilia but not in cytoplasmic microtubules.
    Cell Motil. 1985;5(3):239-49 PMID: 3891093
  13. A rapid single-stranded cloning strategy for producing a sequential series of overlapping clones for use in DNA sequencing: application to sequencing the corn mitochondrial 18 S rDNA.
    Plasmid. 1985 Jan;13(1):31-40 PMID: 3991809
  14. Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence.
    Proc Natl Acad Sci U S A. 1983 Jun;80(12):3548-52 PMID: 6304716
  15. Retention of ciliary ninefold structure after removal of microtubules.
    J Cell Sci. 1989 Mar;92 ( Pt 3):391-402 PMID: 2592445
  16. Relationship between tektins and intermediate filament proteins: an immunological study.
    Cell Motil Cytoskeleton. 1989;14(3):359-71 PMID: 2582496
  17. Methods to define and locate patterns of motifs in sequences.
    Comput Appl Biosci. 1988 Mar;4(1):53-60 PMID: 2898280
  18. Molecular and cellular biology of intermediate filaments.
    Annu Rev Biochem. 1988;57:593-625 PMID: 3052284
  19. Improved tools for biological sequence comparison.
    Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444-8 PMID: 3162770
  20. Amino acid sequences and homopolymer-forming ability of the intermediate filament proteins from an invertebrate epithelium.
    EMBO J. 1988 Oct;7(10):2995-3001 PMID: 3181126
  21. Yeast RNA polymerase II genes: isolation with antibody probes.
    Science. 1983 Nov 18;222(4625):778-82 PMID: 6356359
  22. An interactive graphics program for comparing and aligning nucleic acid and amino acid sequences.
    Nucleic Acids Res. 1982 May 11;10(9):2951-61 PMID: 7099970
  23. Periodic charge distribution in the intermediate filament proteins desmin and vimentin.
    J Mol Biol. 1982 Dec 15;162(3):693-8 PMID: 7166759
  24. Structure and chemical composition of insoluble filamentous components of sperm flagellar microtubules.
    J Cell Sci. 1982 Dec;58:1-22 PMID: 7183681
  25. Differential protein synthesis and utilization during cilia formation in sea urchin embryos.
    Dev Biol. 1977 Dec;61(2):311-29 PMID: 145385
  26. Selective chemical cleavage of tryptophanyl peptide bonds by oxidative chlorination with N-chlorosuccinimide.
    Biochemistry. 1976 Nov 16;15(23):5071-5 PMID: 990266
  27. Conformational properties of amino acid residues in globular proteins.
    J Mol Biol. 1976 Nov 5;107(3):327-56 PMID: 1003471
  28. Evidence for a non-tubulin spindle matrix and for spindle components immunologically related to tektin filaments.
    J Cell Sci. 1992 Apr;101 ( Pt 4):809-22 PMID: 1527181
  29. Molecular characterization of microtubule-associated proteins tau and MAP2.
    Trends Neurosci. 1991 May;14(5):193-9 PMID: 1713721
  30. One motor, many tails: an expanding repertoire of force-generating enzymes.
    Cell. 1990 Mar 23;60(6):883-5 PMID: 2138513
  31. Cross-reactivity of antibodies specific for flagellar tektin and intermediate filament subunits.
    J Cell Biol. 1987 Jun;104(6):1563-8 PMID: 2438286
  32. Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau.
    Nature. 1989 Nov 30;342(6249):498-505 PMID: 2511449
  33. Evidence for tektins in centrioles and axonemal microtubules.
    Proc Natl Acad Sci U S A. 1988 Apr;85(8):2643-7 PMID: 3282233
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.89.18.8567
Published
1992-09-15
Pages
8567-71
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC49961
Subset
IM
Grants
NIGMS NIH HHS · 1F32-GM11669 · United States
NIGMS NIH HHS · GM35648 · United States
Databases
GENBANK
M97188
External Links
PubMed source DOI: 10.1073/pnas.89.18.8567 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