The video explains the structure and function of the 26S proteasome, likening it to a molecular garbage can. It describes how ubiquitinated proteins are targeted for degradation, with the proteasome opening its lid to allow entry. The process involves ATP hydrolysis, which facilitates protein unfolding and cleavage into smaller peptides. The proteasome's unique threonine protease activity is highlighted, emphasizing its role in recycling proteins for amino acid reuse.

What is the primary function of the proteasome in the cell?

• To synthesize new proteins

• To act as a molecular garbage can

• To transport proteins across membranes

• To store energy in the form of ATP

How does the proteasome recognize proteins that need to be degraded?

• By their color

• By their location in the cell

• By their size

• By the presence of a ubiquitin tail

What is polyubiquitination?

• The synthesis of ubiquitin molecules

• The process of adding a single ubiquitin to a protein

• The process of adding multiple ubiquitin molecules to a protein

• The removal of ubiquitin from a protein

What role does ATP play in the function of the proteasome?

• It provides energy for protein synthesis

• It acts as a substrate for protein degradation

• It facilitates the unfolding of proteins

• It binds to proteins to mark them for degradation

Which type of protease is primarily involved in the proteasome's cleavage mechanism?

• Threonine protease

• Serine protease

• Cysteine protease

• Aspartate protease

What happens to the ubiquitin molecules during the protein degradation process?

• They are degraded along with the protein

• They are recycled and reused

• They are converted into amino acids

• They are stored in the proteasome

What is the final product released from the proteasome after protein degradation?

• Nucleic acids

• Small peptides

• Large protein complexes

• Individual amino acids