Publications by authors named "Huma Rahil"
Article Synopsis
- - Protein synthesis starts with the creation of a ribosome-mRNA complex, where the small ribosomal subunit (30) binds to mRNAs by recognizing the Shine-Dalgarno (SD) sequence.
- - Research techniques like cryo-electron microscopy and mass spectrometry were used to investigate how bS1 protein helps deliver mRNA to the ribosome, facilitating the necessary interactions for translation to begin.
- - The study highlights the roles of bS1 and RNA polymerase (RNAP) in enhancing translation initiation, emphasizing how these components work together to link transcription and translation processes.
Lesions and stable secondary structures in mRNA severely impact the translation efficiency, causing ribosome stalling and collisions. Prokaryotic ribosomal proteins Rps3, Rps4 and Rps5, located in the mRNA entry tunnel, form the mRNA helicase center and unwind stable mRNA secondary structures during translation. However, the mechanism underlying the detection of lesions on translating mRNA is unclear.
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- Protein synthesis starts when the ribosome binds to mRNA, with the 30S ribosomal subunit being crucial for this process in bacteria, aided by the Shine Dalgarno (SD) sequence.
- Research using advanced techniques like cryo-EM and mass spectrometry reveals that ribosomal protein bS1 helps deliver mRNA to the ribosome, facilitating the formation of the SD duplex and activating the 30S subunit.
- The study also shows that bS1 enhances translation initiation in collaboration with RNA polymerase (RNAP), illustrating the interaction between the SD duplex, ribosomal proteins, and RNAP in linking transcription and translation.
The SARS-CoV-2 non-structural protein 1 (Nsp1) contains an N-terminal domain and C-terminal helices connected by a short linker region. The C-terminal helices of Nsp1 (Nsp1-C-ter) from SARS-CoV-2 bind in the mRNA entry channel of the 40S ribosomal subunit and blocks mRNA entry, thereby shutting down host protein synthesis. Nsp1 suppresses host immune function and is vital for viral replication.
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