Sandbox Reserved 327: Difference between revisions
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==eIF1-eIF5 binding sites== | ==eIF1-eIF5 binding sites== | ||
There are two | There are two | ||
<scene name='Sandbox_Reserved_327/Basic_eif1/3'>eIF1-eIF5 binding sites</scene>: at the NTT site of eIF1 and at a KH surface area, a specific region that rich in Lysine (K) and hydrophobic (H) residues <ref name="eIF1"/>. These bindings are different from the eIF1-ribosome binding site and are salt dependent, with high salt concentration would make the interaction weaker <ref name="eIF1"/>. The eIF1-NTT area is believed to play role in stimulating the MFC assembly by promoting the eIF5- eIF2β <ref name="eIF1"/>. The other binding site area | <scene name='Sandbox_Reserved_327/Basic_eif1/3'>eIF1-eIF5 binding sites</scene>: at the NTT site of eIF1 and at a KH surface area, a specific region that rich in Lysine (K) and hydrophobic (H) residues <ref name="eIF1"/>. These bindings are different from the eIF1-ribosome binding site and are salt dependent, with high salt concentration would make the interaction weaker <ref name="eIF1"/>. | ||
===eIF1-NTT=== | |||
The eIF1-NTT area is believed to play role in stimulating the MFC assembly by promoting the eIF5- eIF2β <ref name="eIF1"/>. | |||
''In vitro'' mutation in the eIF1-NTT area would alter the binding of eIF5 and eIF2β, but not eIF3c which supported that this area played role in stimulating the MFC assembly <ref name="eIF1"/>. ''In vivo'' study also supported that eIF1-NTT would allow the binding of eIF1 to the eIF5 and eIF2β <ref name="eIF1"/>. | |||
===eIF1-KH=== | |||
The other binding site area of eIF1 to eIF5 which is believed to play role in the AUG start codon selection since ''in vitro'' mutation in this area by altering the basic/hydrophobic part of the KH region would relax the start codon selection <ref name="eIF1"/>.The mutation would also alter the formation of MFC, but not like mutation in the eIF1-NTT area, eIF1-NTT mutation is lethal to the yeast growth <ref name="eIF1"/>. | |||
=Function and Mechanism= | =Function and Mechanism= |