Difficulty: Easy
Correct Answer: The 7-methylguanosine (m7G) cap at the 5′ end of the mRNA
Explanation:
Introduction:Eukaryotic translation initiation relies on recognition of the 5′ cap structure by cap-binding factors, which recruit the small ribosomal subunit to scan for the start codon. This differs from bacteria, which use base-pairing between the Shine–Dalgarno sequence and 16S rRNA.
Given Data / Assumptions:
Concept / Approach:
The cap-dependent scanning model posits that the small subunit (40S) is recruited to the mRNA via eIF4E recognition of the m7G cap. The preinitiation complex then scans 5′→3′ to locate an AUG in a favorable Kozak context. Some specialized mRNAs use IRES elements, but these are exceptions.
Step-by-Step Solution:
Cap-binding protein eIF4E recognizes the m7G cap.Scaffold eIF4G bridges to additional factors and the 40S subunit.The 43S preinitiation complex binds and scans to the start codon.Upon AUG recognition, large subunit joining completes initiation.Verification / Alternative check:
Biochemical reconstitution shows cap dependence for most cellular mRNAs; cap analogs competitively inhibit initiation, confirming the central role of the m7G cap.
Why Other Options Are Wrong:
Shine–Dalgarno is bacterial, not eukaryotic. tRNA alone cannot mediate mRNA binding. The poly(A) tail aids initiation but is not sufficient by itself. IRES elements are not universal.
Common Pitfalls:
Assuming that all eukaryotic mRNAs use IRES or that the poly(A) tail replaces the cap in typical initiation.
Final Answer:
The 7-methylguanosine (m7G) cap at the 5′ end of the mRNA
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