Open AccessUntersuchung von Hitzeschock‐Proteinen bei Tardigraden im aktiven gegenüber anhydrobiotischen Zustand mit Hilfe von Proteomics‐Techniken
Author(s) -
Schokraie Elham,
HotzWagenblatt Agnes,
Warnken Uwe,
Frohme Marcus,
Dandekar Thomas,
Schill Ralph O.,
Schnölzer Martina
Publication year - 2011
Publication title -
journal of zoological systematics and evolutionary research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.769
H-Index - 50
eISSN - 1439-0469
pISSN - 0947-5745
DOI - 10.1111/j.1439-0469.2010.00608.x
Subject(s) - heat shock protein , hsp60 , hsp70 , chaperone (clinical) , proteomics , biology , microbiology and biotechnology , biochemistry , chemistry , medicine , pathology , gene
Abstract The eutardigrade Milnesium tardigradum can undergo cryptobiosis and can survive extreme environmental conditions. However, the survival mechanisms of tardigrades are still poorly understood. Heat shock proteins (Hsps) as an important subgroup of chaperones which protect proteins from irreversible aggregation and degradation might play an important role in anhydrobiosis. In this report, we therefore investigated Hsps in tardigrades in the active versus the anhydrobiotic state employing proteomics techniques. Protein lysates from tardigrades in both states were separated by one‐dimensional gel electrophoresis, in‐gel digested with trypsin and tryptic peptides were analyzed by high sensitive nanoLC‐ESI‐MS/MS on a LTQ‐Orbitrap mass spectrometer. This study indicates the presence of Hsps of the major chaperone families Hsp40, Hsp60, Hsp70, Hsp90, small Hsps and furthermore nucleotide exchange factors and co‐chaperones in Milnesium tardigradum . A comparative analysis of the identified Hsps in both states was performed by calculating the exponentially modified protein abundance index.