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

The Journal of Experimental Biology
Heli HavukainenØyvind Halskau

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 nipp...Continue Reading

References

Jan 1, 1990·Archives of Insect Biochemistry and Physiology·D E Wheeler, J K Kawooya
Aug 1, 1989·Archives of Biochemistry and Biophysics·M Benore-ParsonsL P Wennogle
Apr 8, 1998·The Journal of Peptide Research : Official Journal of the American Peptide Society·K BarlosS Koutsogianni
Apr 16, 1998·Insect Biochemistry and Molecular Biology·G Don-Wheeler, F Engelmann
Feb 17, 1999·Proceedings of the National Academy of Sciences of the United States of America·J WalterC Haass
May 23, 2002·Biochemistry·A Keith DunkerZoran Obradović
Jul 12, 2002·Insect Biochemistry and Molecular Biology·Mário A C Silva-NetoHatisaburo Masuda
Dec 14, 2002·Biochemical and Biophysical Research Communications·Do Hoon KimWoo Keun Song
Jan 23, 2003·Bioinformatics·Jens P LingeMichael Nilges
Feb 5, 2003·Proceedings of the National Academy of Sciences of the United States of America·Gro V AmdamStig W Omholt
Mar 26, 2003·Insect Biochemistry and Molecular Biology·M D PiulachsX Bellés
Jul 24, 2003·Journal of Theoretical Biology·Gro Vang Amdam, Stig W Omholt
Apr 13, 2004·Protein Science : a Publication of the Protein Society·Michael B HowardRonald M Weiner
Apr 15, 2004·Genetics·Melanie A Huntley, G Brian Golding
Jan 18, 2005·Journal of the American Society for Mass Spectrometry·Justin G StrohJulie Xie
Mar 2, 2005·Nature Reviews. Molecular Cell Biology·H Jane Dyson, Peter E Wright
Aug 9, 2005·Journal of Pharmaceutical and Biomedical Analysis·Thomas R SharpJustin G Stroh
Jan 19, 2006·Proceedings of the National Academy of Sciences of the United States of America·Siri-Christine SeehuusGro V Amdam
Aug 1, 2006·Molecular Biology and Evolution·Melanie A Huntley, G Brian Golding
Dec 7, 2006·Journal of Lipid Research·Marcel M W SmolenaarsDick J Van der Horst
Mar 8, 2007·PLoS Biology·C Mindy NelsonGro V Amdam
Sep 15, 2007·The American Naturalist·Gro V AmdamKlaus Hartfelder
Feb 16, 2008·Invertebrate Neuroscience : in·Rachel Denison, Valérie Raymond-Delpech
Jun 25, 2008·Annual Review of Biophysics·Vladimir N UverskyA Keith Dunker
Sep 16, 2008·Journal of Insect Physiology·Muhammad Tufail, Makio Takeda
Sep 17, 2008·Current Protocols in Bioinformatics·Julie D ThompsonDes G Higgins

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Citations

Jul 24, 2014·Archives of Insect Biochemistry and Physiology·Mayura VeeranaLertluk Ngernsiri
Sep 27, 2018·Bioscience Reports·Lin ChaiZhicheng Fang
Nov 23, 2019·Current Protein & Peptide Science·Le CuiKai Guan
Mar 17, 2015·Intrinsically Disordered Proteins·Vladimir N Uversky
Jul 31, 2013·The Journal of Biological Chemistry·Heli HavukainenGro V Amdam

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