A vitellogenin polyserine cleavage site: Highly disordered conformation protected from proteolysis by phosphorylation

Heli Havukainen, Jarl Underhaug, Florian Wolschin, Gro Amdam, Øyvind Halskau

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Vitellogenin (Vg) is an egg-yolk precursor protein in most oviparous species. In honeybee (Apis mellifera), the protein (AmVg) also affects social behavior and life-span plasticity. Despite its manifold functions, the AmVg molecule remains poorly understood. The subject of our structure-oriented AmVg study is its polyserine tract - a little-investigated repetitive protein segment mostly found in insects. We previously reported that AmVg is tissue specifically cleaved in the vicinity of this tract. Here, we show that, despite its potential for an open, disordered structure, AmVg is unexpectedly resistant to trypsin/chymotrypsin digestion at the tract. Our findings suggest that multiple phosphorylation plays a role in this resilience. Sequence variation is highly pronounced at the polyserine region in insect Vgs. We demonstrate that sequence differences in this region can lead to structural variation, as NMR and circular dichroism (CD) evidence assign different conformational propensities to polyserine peptides from the honeybee and the jewel wasp Nasonia vitripennis; the former is extended and disordered and the latter more compact and helical. CD analysis of the polyserine region of bumblebee Bombus ignitus and wasp Pimpla nipponica supports a random coil structure in these species. The spectroscopic results strengthen our model of the AmVg polyserine tract as a flexible domain linker shielded by phosphorylation.

Original languageEnglish (US)
Pages (from-to)1837-1846
Number of pages10
JournalJournal of Experimental Biology
Volume215
Issue number11
DOIs
StatePublished - Jun 2012

Fingerprint

Vitellogenins
vitellogenin
proteolysis
cleavage
Proteolysis
circular dichroism spectroscopy
phosphorylation
honeybee
Phosphorylation
Bombus
wasp
honey bees
protein
Pimpla
Wasps
insect
Nasonia vitripennis
Circular Dichroism
insects
proteins

Keywords

  • Honeybee
  • NMR
  • Phosphorylation
  • Polyserine linker
  • Vitellogenin

ASJC Scopus subject areas

  • Animal Science and Zoology
  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Physiology
  • Insect Science
  • Aquatic Science

Cite this

A vitellogenin polyserine cleavage site : Highly disordered conformation protected from proteolysis by phosphorylation. / Havukainen, Heli; Underhaug, Jarl; Wolschin, Florian; Amdam, Gro; Halskau, Øyvind.

In: Journal of Experimental Biology, Vol. 215, No. 11, 06.2012, p. 1837-1846.

Research output: Contribution to journalArticle

Havukainen, Heli ; Underhaug, Jarl ; Wolschin, Florian ; Amdam, Gro ; Halskau, Øyvind. / A vitellogenin polyserine cleavage site : Highly disordered conformation protected from proteolysis by phosphorylation. In: Journal of Experimental Biology. 2012 ; Vol. 215, No. 11. pp. 1837-1846.
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