Proteasome

What mark does the cell put on a protein to send it to the 26S proteasome?

Why does the proteasome keep its cutting sites inside a sealed barrel?

Which part of the 26S proteasome grips, unfolds and pulls the tagged protein into the barrel?

What does Rpn11, a zinc enzyme of the proteasome lid, do to the substrate?

Which three beta subunits of the proteasome core particle carry the active sites?

The proteasome core particle has 28 subunits in ?blank: (alpha1-7 beta1-7)2.

Why is the proteasome's HbYX gate signal thought to be older than the 26S particle itself?

How does a PROTAC get the proteasome to destroy a chosen protein?

Ubiquitin binding alone does not commit a protein to the proteasome. What does?

Rpn11 cuts the ubiquitin chain off faster when ?blank.

How do the proteasome's ATPases open the gate into the core particle?

The six proteasome ATPases stand in a spiral staircase. Why does the substrate chain move one way only?

In the proteasome's ATPase staircase, what does the subunit at the bottom do next?

In each proteasome ATPase, a ?blank driven by ATP hydrolysis sets when that subunit holds or releases the chain.

Which residue in the proteasome's active beta subunits attacks the peptide bond?

What decides when peptides leave the proteasome barrel, according to Kisselev and colleagues' proposal?

An adult human breaks down and rebuilds about ?blank of body protein a day, but eats only 50–80 g.

Most proteasome peptides become amino acids for new proteins. What happens to a few of them?

In mouse L929 cells, how does the number of proteins the proteasomes destroy per minute compare with the number the ribosomes make?

Where does the analogy 'the proteasome is a paper shredder' break down about how input gets in?

Unlike a recycling plant, the proteasome also destroys healthy proteins on schedule. What does that let the cell do?

One mouse 26S proteasome needs about ?blank to degrade one ubiquitinated DHFR molecule (Ub5-DHFR).

How did Peth and colleagues get the 13 s a proteasome needs per Ub5-DHFR molecule?

Mouse 26S proteasomes spend ?blank ATP to destroy one Ub5-DHFR molecule.

Folic acid stabilises the DHFR fold. What happened to proteasome ATP use per minute and to degradation time when it was bound?

Blocking ATP binding in one yeast proteasome ATPase (Rpt3, Rpt5 or Rpt6) cut basal ATP use by about 66%, not the 16% expected. What does that show?

In cryo-EM of working yeast 26S proteasomes, how far does the substrate move per ATP?

The human 26S proteasome is often given as 2.5 MDa, citing Dong et al. 2019. What is the problem with that source?