Practice Questions

Plant Golgi bodies are often referred to as dictyosomes because they exist as smaller, dispersed stacks within the plant cytoplasm.

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41. The cell structure acting as the principal finishing, sorting, and packaging factory for newly synthesized secretory proteins is the

A. Smooth endoplasmic reticulum
B. Golgi apparatus
C. Nucleolus
D. Mitochondrion

The Golgi apparatus accepts vesicles from the ER, performs biochemical modifications, and targets them to their final cellular destinations.

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40. The biochemical assembly of new cellular lipid bilayers takes place on the

A. Luminal face of the rough ER
B. Cytosolic face of the smooth ER
C. Interior matrix of the mitochondria
D. Exoplasmic leaflet of the Golgi

The active sites of lipid synthesis enzymes face the cytosol, adding new lipid molecules directly to the cytosolic leaflet of the SER.

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Ribophorins I and II are structural glycoproteins found uniquely on the RER membrane that secure ribosomes in place during synthesis.

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38. A block in the budding pathway of COPII vesicles from the endoplasmic reticulum causes a cellular accumulation of

A. Free lipids in the nucleoplasm
B. Newly synthesized proteins inside the ER lumen
C. Lysosomal enzymes in the extracellular matrix
D. Active ribosomes in the peroxisome

Because COPII vesicles carry cargo forward (anterograde), blocking them causes proteins to pile up within the ER.

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37. The membrane-bound enzyme responsible for freeing glucose-6-phosphate into pure glucose within human liver cells during glycogenolysis is located inside the

A. Mitochondrial matrix
B. Lysosomal core
C. Smooth endoplasmic reticulum
D. Golgi trans-cisternae

Glucose-6-phosphatase is a resident enzyme of the SER membrane, playing a key role in regulating blood glucose levels.

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36. In cells treated with a drug that selectively blocks the activity of the Sec61 translocon complex, the direct downstream operational failure observed is the

A. Inability to package lipids into transport vesicles
B. Failure of nascent proteins to enter the rough ER lumen
C. Arrest of mRNA export from the nuclear pores
D. Inhibition of ATP synthase assembly in cristae

The Sec61 complex forms the physical protein-conducting channel (translocon) across the RER membrane. Blocking it halts co-translational translocation.

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35. The molecular chaperone protein BiP assists protein maturation within the rough endoplasmic reticulum lumen by recognizing and binding to

A. Exposed hydrophobic patches on unfolded polypeptides
B. Terminal mannose-6-phosphate residue networks
C. The hydrophilic N-terminal signal sequence
D. O-linked oligosaccharide modifications

BiP (Binding Immunoglobulin Protein) uses ATP to mask exposed hydrophobic regions on nascent proteins, preventing aggregation and helping them fold properly.

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34. During the process of lipid synthesis in the smooth endoplasmic reticulum, the mechanism that ensures symmetric expansion of both leaflets of the bilayer is the action of

A. ATP-dependent flippases
B. ATP-independent scramblases
C. Passive lipid diffusion pathways
D. Vesicular transport loops

New lipids are added to the cytosolic leaflet of the ER. Scramblases flip lipids randomly across leaflets without needing energy, balancing out the bilayer surface area.

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33. The transport of proteins containing a hydrophobic signal peptide into the RER is halted temporarily in the cytosol by the action of the

A. Nuclear import factor
B. Signal Recognition Particle
C. Ubiquitin ligase system
D. Chaperonin folding cage

The Signal Recognition Particle halts translation temporarily to prevent premature protein folding in the cytosol before docking at the RER translocon.

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