Evolution of the vertebrate beaded filament protein, Bfsp2

comparing the in vitro assembly properties of a "tailed" zebrafish Bfsp2 to its "tailless" human orthologue

Bo Qu, Andrew Landsbury, Helia Berrit Schoenthaler, Ralf Dahm, Yizhi Liu, John I. Clark, Alan R. Prescott, Roy A. Quinlan

    Research output: Contribution to journalArticle

    4 Citations (Scopus)

    Abstract

    In bony fishes, Bfsp2 orthologues are predicted to possess a C-terminal tail domain, which is absent from avian, amphibian and mammalian Bfsp2 sequences. These sequences, are however, not conserved between fish species and therefore questions whether they have a functional role. For other intermediate filament proteins, the C-terminal tail domain is important for both filament assembly and regulating interactions between filaments. We confirm that zebrafish has a single Bfsp2 gene by radiation mapping. Two transcripts (bfsp2 alpha and bfsp2 beta) are produced by alternative splicing of the last exon. Using a polyclonal antibody specific to a tridecameric peptide in the C-terminal tail domain common to both zebrafish Bfsp2 splice variants, we have confirmed its expression in zebrafish lens fibre cells. We have also determined the in vitro assembly properties of zebrafish Bfsp2 alpha and conclude that the C-terminal sequences are required to regulate not only the diameter and uniformity of the in vitro assembly filaments, but also their filament filament associations in vitro. Therefore we conclude zebrafish Bfsp2 alpha is a functional orthologue conforming more closely to the conventional domain structure of intermediate filament proteins. Data mining of the genome databases suggest that the loss of this tail domain could occur in several stages leading eventually to completely tailless orthologues, such as human BFSP2. (C) 2011 Elsevier Ltd. All rights reserved.

    Original languageEnglish
    Pages (from-to)192-202
    Number of pages11
    JournalExperimental Eye Research
    Volume94
    Issue number1
    DOIs
    Publication statusPublished - Jan 2012

    Keywords

    • lens
    • cytoskeleton
    • beaded filaments
    • BFSP1
    • intermediate filament
    • evolution
    • FIBER CELL CYTOSKELETON
    • FIBRILLARY ACIDIC PROTEIN
    • ALPHA-B-CRYSTALLIN
    • EYE LENS
    • INTERMEDIATE-FILAMENTS
    • OPTICAL-PROPERTIES
    • VIMENTIN
    • CP49
    • PHOSPHORYLATION
    • DIFFERENTIATION

    Cite this

    Qu, Bo ; Landsbury, Andrew ; Schoenthaler, Helia Berrit ; Dahm, Ralf ; Liu, Yizhi ; Clark, John I. ; Prescott, Alan R. ; Quinlan, Roy A. / Evolution of the vertebrate beaded filament protein, Bfsp2 : comparing the in vitro assembly properties of a "tailed" zebrafish Bfsp2 to its "tailless" human orthologue. In: Experimental Eye Research. 2012 ; Vol. 94, No. 1. pp. 192-202.
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    abstract = "In bony fishes, Bfsp2 orthologues are predicted to possess a C-terminal tail domain, which is absent from avian, amphibian and mammalian Bfsp2 sequences. These sequences, are however, not conserved between fish species and therefore questions whether they have a functional role. For other intermediate filament proteins, the C-terminal tail domain is important for both filament assembly and regulating interactions between filaments. We confirm that zebrafish has a single Bfsp2 gene by radiation mapping. Two transcripts (bfsp2 alpha and bfsp2 beta) are produced by alternative splicing of the last exon. Using a polyclonal antibody specific to a tridecameric peptide in the C-terminal tail domain common to both zebrafish Bfsp2 splice variants, we have confirmed its expression in zebrafish lens fibre cells. We have also determined the in vitro assembly properties of zebrafish Bfsp2 alpha and conclude that the C-terminal sequences are required to regulate not only the diameter and uniformity of the in vitro assembly filaments, but also their filament filament associations in vitro. Therefore we conclude zebrafish Bfsp2 alpha is a functional orthologue conforming more closely to the conventional domain structure of intermediate filament proteins. Data mining of the genome databases suggest that the loss of this tail domain could occur in several stages leading eventually to completely tailless orthologues, such as human BFSP2. (C) 2011 Elsevier Ltd. All rights reserved.",
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    Evolution of the vertebrate beaded filament protein, Bfsp2 : comparing the in vitro assembly properties of a "tailed" zebrafish Bfsp2 to its "tailless" human orthologue. / Qu, Bo; Landsbury, Andrew; Schoenthaler, Helia Berrit; Dahm, Ralf; Liu, Yizhi; Clark, John I.; Prescott, Alan R.; Quinlan, Roy A.

    In: Experimental Eye Research, Vol. 94, No. 1, 01.2012, p. 192-202.

    Research output: Contribution to journalArticle

    TY - JOUR

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    T2 - comparing the in vitro assembly properties of a "tailed" zebrafish Bfsp2 to its "tailless" human orthologue

    AU - Qu, Bo

    AU - Landsbury, Andrew

    AU - Schoenthaler, Helia Berrit

    AU - Dahm, Ralf

    AU - Liu, Yizhi

    AU - Clark, John I.

    AU - Prescott, Alan R.

    AU - Quinlan, Roy A.

    N1 - Copyright © 2011 Elsevier Ltd. All rights reserved.

    PY - 2012/1

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    N2 - In bony fishes, Bfsp2 orthologues are predicted to possess a C-terminal tail domain, which is absent from avian, amphibian and mammalian Bfsp2 sequences. These sequences, are however, not conserved between fish species and therefore questions whether they have a functional role. For other intermediate filament proteins, the C-terminal tail domain is important for both filament assembly and regulating interactions between filaments. We confirm that zebrafish has a single Bfsp2 gene by radiation mapping. Two transcripts (bfsp2 alpha and bfsp2 beta) are produced by alternative splicing of the last exon. Using a polyclonal antibody specific to a tridecameric peptide in the C-terminal tail domain common to both zebrafish Bfsp2 splice variants, we have confirmed its expression in zebrafish lens fibre cells. We have also determined the in vitro assembly properties of zebrafish Bfsp2 alpha and conclude that the C-terminal sequences are required to regulate not only the diameter and uniformity of the in vitro assembly filaments, but also their filament filament associations in vitro. Therefore we conclude zebrafish Bfsp2 alpha is a functional orthologue conforming more closely to the conventional domain structure of intermediate filament proteins. Data mining of the genome databases suggest that the loss of this tail domain could occur in several stages leading eventually to completely tailless orthologues, such as human BFSP2. (C) 2011 Elsevier Ltd. All rights reserved.

    AB - In bony fishes, Bfsp2 orthologues are predicted to possess a C-terminal tail domain, which is absent from avian, amphibian and mammalian Bfsp2 sequences. These sequences, are however, not conserved between fish species and therefore questions whether they have a functional role. For other intermediate filament proteins, the C-terminal tail domain is important for both filament assembly and regulating interactions between filaments. We confirm that zebrafish has a single Bfsp2 gene by radiation mapping. Two transcripts (bfsp2 alpha and bfsp2 beta) are produced by alternative splicing of the last exon. Using a polyclonal antibody specific to a tridecameric peptide in the C-terminal tail domain common to both zebrafish Bfsp2 splice variants, we have confirmed its expression in zebrafish lens fibre cells. We have also determined the in vitro assembly properties of zebrafish Bfsp2 alpha and conclude that the C-terminal sequences are required to regulate not only the diameter and uniformity of the in vitro assembly filaments, but also their filament filament associations in vitro. Therefore we conclude zebrafish Bfsp2 alpha is a functional orthologue conforming more closely to the conventional domain structure of intermediate filament proteins. Data mining of the genome databases suggest that the loss of this tail domain could occur in several stages leading eventually to completely tailless orthologues, such as human BFSP2. (C) 2011 Elsevier Ltd. All rights reserved.

    KW - lens

    KW - cytoskeleton

    KW - beaded filaments

    KW - BFSP1

    KW - intermediate filament

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    KW - FIBER CELL CYTOSKELETON

    KW - FIBRILLARY ACIDIC PROTEIN

    KW - ALPHA-B-CRYSTALLIN

    KW - EYE LENS

    KW - INTERMEDIATE-FILAMENTS

    KW - OPTICAL-PROPERTIES

    KW - VIMENTIN

    KW - CP49

    KW - PHOSPHORYLATION

    KW - DIFFERENTIATION

    U2 - 10.1016/j.exer.2011.12.001

    DO - 10.1016/j.exer.2011.12.001

    M3 - Article

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    SP - 192

    EP - 202

    JO - Experimental Eye Research

    JF - Experimental Eye Research

    SN - 0014-4835

    IS - 1

    ER -