Answer:
Cofilin binds to older actin filaments
Explanation:
Microfilaments (also called actin filaments) are a class of protein filament common to all eukaryotic cells, which consist of two strands of subunits of the protein actin. Microfilaments form part of the cell's cytoskeleton and interact with the protein myosin in order to allow the movement of the cell. Within the cell, actin may show two different forms: monomeric G-actin and polymeric F-actin filaments. Microfilaments provide shape to the cell because these filaments can depolymerize (disassemble) and polymerize (assembly) quickly, thereby allowing the cell to change its shape. During the polymerization process, the ATP that is bound to G-actin is hydrolyzed to ADP, which is bound to F-actin. ATP-actin subunits are present at the barbed ends of the filaments, and cleavage of the ATP molecules produces highly stable filaments bound to ADP. In consequence, it is expected that cofilin binds preferentially to highly stable (older) filaments ADP-actin filaments instead of ATP-actin filaments.
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Yes, deletion of the possible control elements can cause reduction in reporter gene expression. Due to deletion of a control element, the activator cannot bind to the enhancer. This causes reduction in the gene expression.
Answer: Deletion of element no. 3 causes a reduction in reporter gene expression.
Answer:
The most appropriate answer would be The cell will not make functional proteins from that mRNA strand.
The amino acid sequence of the proteins is derived from the nucleotide sequence of the mRNA (messenger ribonucleotide).
If the sequence of mRNA is miscopied, it will change the sequence of amino acids of the protein.
Consequently, the protein may become non-functional.
