Attempt to optimize some properties of fluorescent chimeras of human small heat shock protein HspB1 by modifying linker length and nature

Biochemistry. Biokhimii︠a︡
Petr N DatskevichNikolai B Gusev

Abstract

Chimerical proteins consisting of enhanced yellow fluorescent protein (EYFP) connected by linkers of different length and nature to the N-terminal end of small heat shock protein HspB1 were obtained and characterized. To obtain fluorescent chimeras with properties similar to those of unmodified small heat shock protein, we used either 12-residue-long linkers of different nature (highly flexible Gly-Ser linker (L1), rigid α-helical linker (L2), or rigid Pro-Ala linker (L3)) or highly flexible Gly-Ser linker consisting of 12, 18, or 21 residues. The wild-type HspB1 formed large stable oligomers consisting of more than 20 subunits. Independent of the length or the nature of the linker, all the fluorescent chimeras formed small (5-9 subunits) oligomers tending to dissociate at low protein concentration. Chaperone-like activity of the wild-type HspB1 and its fluorescent chimeras were compared using lysozyme as a model protein substrate. Under the conditions used, all the fluorescent chimeras possessed higher chaperone-like activity than the wild-type HspB1. Chaperone-like activity of fluorescent chimeras with L1 and L3 linkers was less different from that of the wild-type HspB1 compare to the chaperone-like activity of chimeras with...Continue Reading

References

May 9, 2001·Biochimica Et Biophysica Acta·W C BoelensW W de Jong
Jun 25, 2003·Cell Stress & Chaperones·Guido KappéWilfried W de Jong
Nov 5, 2003·The Journal of Biological Chemistry·Xiankui SunRainer Benndorf
Oct 18, 2005·Biochemical and Biophysical Research Communications·Jean-Marc FontaineMichael J Welsh
Aug 29, 2006·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Jean-Marc FontaineRainer Benndorf
Mar 27, 2009·BMC Biotechnology·Dmitry ShcherboDmitriy M Chudakov
Aug 4, 2009·Journal of Molecular Biology·C BagnérisC Slingsby
Sep 1, 2009·Proceedings of the National Academy of Sciences of the United States of America·Nomalie JayaElizabeth Vierling
Mar 18, 2010·Experimental Cell Research·Catherine PaulAndré-Patrick Arrigo
Apr 6, 2011·Proceedings of the National Academy of Sciences of the United States of America·Stefan JehleRachel E Klevit
Oct 21, 2011·Physiological Reviews·Evgeny V MymrikovNikolai B Gusev
Nov 8, 2011·Protein Science : a Publication of the Protein Society·Barbara Lelj-Garolla, A Grant Mauk
Nov 22, 2011·Protein Expression and Purification·Petr N DatskevichNikolai B Gusev
Jun 12, 2012·The International Journal of Biochemistry & Cell Biology·G WettsteinPh Bonniaud
Jul 19, 2012·Current Molecular Medicine·A-P Arrigo, B Gibert
Oct 3, 2012·Advanced Drug Delivery Reviews·Xiaoying ChenWei-Chiang Shen
Nov 28, 2012·The International Journal of Biochemistry & Cell Biology·Alim S Seit-NebiNikolai B Gusev
Jan 24, 2013·FEBS Letters·Scott P Delbecq, Rachel E Klevit
Feb 6, 2013·Biochemistry. Biokhimii︠a︡·P N DatskevichN B Gusev
Mar 27, 2013·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Serena CarraAngelo Poletti
Oct 22, 2013·PloS One·Jonathan CroweJonathan L E Dean
Jun 29, 2014·Biochimica Et Biophysica Acta·Dezerae CoxHeath Ecroyd

❮ Previous
Next ❯

Citations


❮ Previous
Next ❯

Related Concepts

Related Feeds

Bacterial Cell Wall Structure (ASM)

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

Bacterial Cell Wall Structure

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.