Analysis of distinct molecular assembly complexes of keratin K8 and K18 by hydrogen-deuterium exchange.
PBN-AR
Instytucja
Instytut Biochemii i Biofizyki Polskiej Akademii Nauk
Źródłowe zdarzenia ewaluacyjne
Informacje podstawowe
Główny język publikacji
EN
Czasopismo
Journal of Structural Biology 
ISSN
1047-8477
EISSN
1095-8657
Wydawca
Elsevier
DOI
Rok publikacji
2015
Numer zeszytu
3
Strony od-do
426-440
Numer tomu
192
Identyfikator DOI
Liczba arkuszy
Słowa kluczowe
EN
Cytoskeleton;
Electron microscopy (EM);
Hydrogen–deuterium exchange;
Intermediate filament;
Keratin
Streszczenia
Język
EN
Treść
Keratins are intermediate filament (IF) proteins that form complex filament systems in epithelial cells, thus serving as scaffolding elements and mechanical stress absorbers. The building blocks of keratin IFs are parallel coiled-coil dimers of two distinct sequence-related proteins distinguished as type I and type II keratins. To gain more insight into their structural dynamics, we resorted to hydrogen-deuterium exchange mass spectrometry of keratins K8 and K18, which are characteristic for simple epithelial cells. Using this powerful technique not employed with IFs before, we mapped patterns of protected versus unprotected regions in keratin complexes at various assembly levels. In particular, we localized protein segments exhibiting different hydrogen exchange patterns in tetramers versus filaments. We observed a general pattern of precisely positioned regions of stability intertwining with flexible regions, mostly represented by the non-α-helical segments. Notably, some regions within the coiled-coil domains are significantly more dynamic than others, while the IF-consensus motifs at the end domains of the central α-helical "rod" segment, which mediate the "head-to-tail" dimer-dimer interaction in the filament elongation process, become distinctly more protected upon formation of filaments. Moreover, to gain more insight into the dynamics of the individual keratins, we investigated the properties of homomeric preparations of K8 and K18. The physiological importance of keratins without a partner is encountered in both pathological and experimental situations when one of the two species is present in robust excess or completely absent, such as in gene-targeted mice.
Cechy publikacji
Article
Inne
System-identifier
PX-56b4768a8106eb71826ee7d8
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