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The heat shock protein and the 14-3-3 proteins together form a cytosolic guidance complex that makes it easier for the chloroplast polypeptide to get imported into the chloroplast. [ 43 ] Alternatively, if a chloroplast preprotein's transit peptide is not phosphorylated, a chloroplast preprotein can still attach to a heat shock protein or Toc159 .
A ribosome is made up of two subunits, a small subunit, and a large subunit. These subunits come together before the translation of mRNA into a protein to provide a location for translation to be carried out and a polypeptide to be produced. [3] The choice of amino acid type to add is determined by a messenger RNA (mRNA) molecule. Each amino ...
In most, but not all cases, nuclear-encoded chloroplast proteins are translated with a cleavable transit peptide that's added to the N-terminus of the protein precursor. Sometimes the transit sequence is found on the C-terminus of the protein, [104] or within the functional part of the protein.
Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recapping. It consists of four phases: initiation, elongation, termination, and recapping.
A diagram of a chloroplast. The TIC and TOC complexes are located on different sides of the chloroplast membrane.. The TIC and TOC complexes are translocons located in the chloroplast of a eukaryotic cell, that is, protein complexes that facilitate the transfer of proteins in and out through the chloroplast's membrane.
In contrast to the Sec pathway which transports proteins in an unfolded manner, the Tat pathway serves to actively translocate folded proteins across a lipid membrane bilayer. In plants, the Tat translocase is located in the thylakoid membrane of the chloroplast , where it acts to export proteins into the thylakoid lumen.
RsfS binds to L14, a protein of the large ribosomal subunit, and thereby blocks joining of the small subunit to form a functional 70S ribosome, slowing down or blocking translation entirely. RsfS proteins are found in almost all eubacteria (but not archaea) and homologs are present in mitochondria and chloroplasts (where they are called C7orf30 ...
The translation rate of chloroplast-encoded proteins is controlled by the presence or absence of assembly partners (control by epistasy of synthesis). [26] This mechanism involves negative feedback through binding of excess protein to the 5' untranslated region of the chloroplast mRNA. [27]