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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10613 - Zoology
Result continuities
Project
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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