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Related Concept Videos

Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
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Two unique membrane-bound AAA proteins from Sulfolobus solfataricus.

Justyna Serek-Heuberger1, Cédric F V Hobel, Stanislaw Dunin-Horkawicz

  • 1Department of Protein Evolution, Max-Planck Institute for Developmental Biology, Spemannstrasse 35, 72076 Tübingen, Germany.

Biochemical Society Transactions
|January 16, 2009
PubMed
Summary

Thermoacidophilic crenarchaea possess unique membrane-bound AAA proteins, MBA1 and MBA2. These proteins form stable ring complexes dependent on their N-terminal extensions.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Extremophile Research

Background:

  • Thermoacidophilic crenarchaea, such as Sulfolobus, utilize a diverse set of AAA (ATPase associated with various cellular activities) proteins.
  • This includes specialized proteins like proteasome-associated ATPases, Vps4 (vacuolar protein sorting 4) homologues, and two distinct Cdc48 (cell-division cycle 48)-like proteins.

Purpose of the Study:

  • To investigate the nature and function of two unique, deeply branching AAA proteins found in Sulfolobus, designated MBA (membrane-bound AAA) 1 and MBA2.
  • To determine their evolutionary relationship, structural features, and assembly into complexes.

Main Methods:

  • Computational analysis and experimental characterization of MBA1 and MBA2.
  • Heterologous expression in Escherichia coli to assess nucleotidase activity.
  • Analysis of ring complex formation and its dependence on N-terminal extensions.

Main Results:

  • MBA1 and MBA2 are divergent AAA proteins, monophyletic, and share a common ancestor with the Cdc48 clade.
  • Both proteins possess two nucleotide-binding domains and lack canonical folded N-terminal domains, featuring instead unstructured N-terminal extensions with a single transmembrane helix.
  • MBA1 and MBA2 are membrane-bound, exhibit nucleotidase activity, and form stable ring complexes, a process contingent on their N-terminal extensions.

Conclusions:

  • MBA1 and MBA2 represent a novel class of membrane-bound AAA proteins in archaea.
  • Their unique structural features and ability to form ring complexes suggest specialized roles in cellular processes within thermoacidophilic environments.
  • The N-terminal extensions are crucial for the assembly and stability of these AAA protein complexes.