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The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence

Sarr, Medoune and Kitoka, Kristine and Walsh-White, Kellie-Ann and Kaldmaee, Margit and Metlans, Rimants and Tars, Kaspar and Mantese, Alessandro and Shah, Dipen and Landreh, Michael and Rising, Anna and Johansson, Jan and Jaudzems, Kristaps and Kronqvist, Nina (2022). The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence. Journal of Biological Chemistry. 298 :5 , 101913
[Research article]

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Abstract

The N-terminal (NT) domain of spider silk proteins (spi-droins) is crucial for their storage at high concentrations and also regulates silk assembly. NTs from the major ampullate spidroin (MaSp) and the minor ampullate spidroin are mono-meric at neutral pH and confer solubility to spidroins, whereas at lower pH, they dimerize to interconnect spidroins in a fiber. This dimerization is known to result from modulation of electrostatic interactions by protonation of well-conserved glutamates, although it is undetermined if this mechanism applies to other spidroin types as well. Here, we determine the solution and crystal structures of the flagelliform spidroin NT, which shares only 35% identity with MaSp NT, and investigate the mechanisms of its dimerization. We show that flagelliform spidroin NT is structurally similar to MaSp NT and that the electrostatic intermolecular interaction between Asp 40 and Lys 65 residues is conserved. However, the protonation events involve a different set of residues than in MaSp, indicating that an overall mechanism of pH-dependent dimerization is conserved but can be mediated by different pathways in different silk types.

Authors/Creators:Sarr, Medoune and Kitoka, Kristine and Walsh-White, Kellie-Ann and Kaldmaee, Margit and Metlans, Rimants and Tars, Kaspar and Mantese, Alessandro and Shah, Dipen and Landreh, Michael and Rising, Anna and Johansson, Jan and Jaudzems, Kristaps and Kronqvist, Nina
Title:The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence
Series Name/Journal:Journal of Biological Chemistry
Year of publishing :2022
Volume:298
Number:5
Article number:101913
Number of Pages:14
Publisher:ELSEVIER
ISSN:0021-9258
Language:English
Publication Type:Research article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Biochemistry and Molecular Biology
URN:NBN:urn:nbn:se:slu:epsilon-p-117576
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-117576
Additional ID:
Type of IDID
DOI10.1016/j.jbc.2022.101913
Web of Science (WoS)000798082100005
ID Code:28606
Faculty:VH - Faculty of Veterinary Medicine and Animal Science
Department:(VH) > Dept. of Anatomy, Physiology and Biochemistry
Deposited By: SLUpub Connector
Deposited On:26 Aug 2022 11:49
Metadata Last Modified:26 Aug 2022 11:51

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