Final answer:
Binding of SRP to a N-terminal signal sequence can transiently arrest translation of a secretory protein by halting elongation while the ribosome-SRP complex finds the ER membrane. After binding to the receptor, the SRP releases and translation resumes.
Step-by-step explanation:
The event that can induce a transient arrest in translation of a secretory protein is the binding of SRP to a N-terminal signal sequence. During the protein synthesis process of secretory proteins, the signal recognition particle (SRP) plays a crucial role in facilitating the translocation of the polypeptide into the endoplasmic reticulum (ER). The SRP identifies the signal sequence as it emerges from the ribosome and binds to it, causing a temporary halt in translation until the ribosome-SRP complex can locate the ER membrane. Once the complex binds to an SRP receptor on the ER membrane, the SRP is released and translation can resume.
The roles of other elements mentioned, such as SRP receptor, signal peptidase, stop-transfer sequence, and snRNPs, differ from the immediate halting of translation. For example, the stop-transfer sequence is involved in the integration of a protein into the membrane but does not directly cause translation to pause. Signal peptidase cleaves the signal sequence but doesn't arrest translation. Similarly, the binding of snRNPs to the large ribosomal unit is part of splicing and does not play a role in translation arrest.