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Conservation of a pH-sensitive structure in the C-terminal region of spider silk extends across the entire silk gene family

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027006%3A_____%2F18%3A00004746" target="_blank" >RIV/00027006:_____/18:00004746 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1038/s41437-018-0050-9" target="_blank" >http://dx.doi.org/10.1038/s41437-018-0050-9</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41437-018-0050-9" target="_blank" >10.1038/s41437-018-0050-9</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Conservation of a pH-sensitive structure in the C-terminal region of spider silk extends across the entire silk gene family

  • Original language description

    Spiders produce multiple silks with different physical properties that allow them to occupy a diverse range of ecological niches, including the underwater environment. Despite this functional diversity, past molecular analyses show a high degree of amino acid sequence similarity between C-terminal regions of silk genes that appear to be independent of the physical properties of the resulting silks; instead, this domain is crucial to the formation of silk fibers. Here, we present an analysis of the C-terminal domain of all known types of spider silk and include silk sequences from the spider Argyroneta aquatica, which spins the majority of its silk underwater. Our work indicates that spiders have retained a highly conserved mechanism of silk assembly, despite the extraordinary diversification of species, silk types and applications of silk over 350 million years. Sequence analysis of the silk C-terminal domain across the entire gene family shows the conservation of two uncommon amino acids that are implicated in the formation of a salt bridge, a functional bond essential to protein assembly. This conservation extends to the novel sequences isolated from A. aquatica. This finding is relevant to research regarding the artificial synthesis of spider silk, suggesting that synthesis of all silk types will be possible using a single process.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10613 - Zoology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2018

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Heredity

  • ISSN

    0018-067X

  • e-ISSN

    1365-2540

  • Volume of the periodical

    120

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    7

  • Pages from-to

    574-580

  • UT code for WoS article

    000431833200007

  • EID of the result in the Scopus database

    2-s2.0-85042068900