medium · MCAT bio-biochem
A protein is found to be glycosylated, sulfated on a tyrosine, and have its signal sequence cleaved. A researcher wants to identify the compartment where tyrosine sulfation occurs, distinguishing it from the other modifications. Tyrosine sulfation is best used as a marker for the:
- trans-Golgi network, because the sulfotransferase that modifies tyrosine residues resides there, downstream of where N-linked glycans are first added
- rough endoplasmic reticulum lumen, where co-translational modifications including signal cleavage and core glycosylation occur
- cis-Golgi, because all sulfation and the trimming of mannose residues both initiate in the earliest Golgi cisterna
- cytosolic face of the smooth ER, where soluble sulfotransferases act on nascent chains before import
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