Hauptseite > Publikationsdatenbank > Conserved structures of ESCRT-III superfamily members across domains of life > print

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037 _ _ |a FZJ-2024-02674
082 _ _ |a 540
100 1 _ |a Schlösser, Lukas
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245 _ _ |a Conserved structures of ESCRT-III superfamily members across domains of life
260 _ _ |a Amsterdam [u.a.]
|c 2023
|b Elsevier Science
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520 _ _ |a Structural and evolutionary studies of cyanobacterial phage shock protein A (PspA) and inner membrane-associated protein of 30 kDa (IM30) have revealed that these proteins belong to the endosomal sorting complex required for transport-III (ESCRT-III) superfamily, which is conserved across all three domains of life. PspA and IM30 share secondary and tertiary structures with eukaryotic ESCRT-III proteins, whilst also oligomerizing via conserved interactions. Here, we examine the structures of bacterial ESCRT-III-like proteins and compare the monomeric and oligomerized forms with their eukaryotic counterparts. We discuss conserved interactions used for self-assembly and highlight key hinge regions that mediate oligomer ultrastructure versatility. Finally, we address the differences in nomenclature assigned to equivalent structural motifs in both the bacterial and eukaryotic fields and suggest a common nomenclature applicable across the ESCRT-III superfamily.
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700 1 _ |a Sachse, Carsten
|0 P:(DE-Juel1)173949
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700 1 _ |a Low, Harry H.
|0 0000-0002-1226-3217
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700 1 _ |a Schneider, Dirk
|0 0000-0003-4517-6387
|b 3
|e Corresponding author
773 _ _ |a 10.1016/j.tibs.2023.08.009
|g Vol. 48, no. 11, p. 993 - 1004
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|t Trends in biochemical sciences
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