[HTML][HTML] Role of C-terminal extensions of subunits β2 and β7 in assembly and activity of eukaryotic proteasomes
PC Ramos, AJ Marques, MK London… - Journal of Biological …, 2004 - ASBMB
A close inspection of the crystal structure of the yeast 20 S proteasome revealed that a
prominent connection between the two β-rings is mediated by the subunit β7/Pre4. Its C-
terminal extension intercalates between the β1/Pre3 and β2/Pup1 subunits on the opposite
ring. We show that the interactions promoted by the β7/Pre4 tail are important to facilitate the
formation of 20 S particles from two half-proteasome precursor complexes and/or to stabilize
mature 20 S proteasomes. The deletion of 19 residues from the β7/Pre4 C terminus leads to …
prominent connection between the two β-rings is mediated by the subunit β7/Pre4. Its C-
terminal extension intercalates between the β1/Pre3 and β2/Pup1 subunits on the opposite
ring. We show that the interactions promoted by the β7/Pre4 tail are important to facilitate the
formation of 20 S particles from two half-proteasome precursor complexes and/or to stabilize
mature 20 S proteasomes. The deletion of 19 residues from the β7/Pre4 C terminus leads to …