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  1. Plaud, Jean
  2. Biblio | LaHDAK Team
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Plaud, Jean

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Free postage Opens image gallery Image not available Photos not available for this variation. Price: EUR 4. Add to basket -. Watch this item Watching Watch list is full. Their binding causes the DNA to bend, bringing them near a gene promoter, even though they may be thousands of base pairs away. Other transcription factor proteins join the activator proteins, forming a protein complex which binds to the gene promoter. This protein complex makes it easier for RNA polymerase to attach to the promoter and start transcribing a gene. Methylation, the addition of a methyl group to the C nucleotides, prevents CTCF from attaching to the insulator, turning it off, allowing the enhancers to bind to the promoter.

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This diagram simplifies the DNA greatly—promoters, enhancers, and insulators can be dozens or even hundreds of base pairs long. Nucleotides are only added to the 3' end of the RNA molecule. A cap and tail are added to the 5' and 3' ends of the new RNA molecule as protection and to help it leave the nucleus. The 5' cap consists of a single G nucleotide. The 3' Poly-A tail consists of hundreds of A nucleotides. Noncoding introns intervening sequences are removed fromthe RNA strand.

The remaining coding segments, or exons expressed sequences are joined together. The 5' cap can then be recognized by a nuclear pore complex, allowing the mRNA to leave the nucleus. The 5' cap makes it so both ends of the mRNA are 3', protecting it from exonucleases which target 5' ends. Each amino acid has its own tRNA molecule with the anticodon for that amino acid.

A small ribosomal subunit attaches itself to the 5' end of an mRNA strand. It moves along the mRNA until it finds a start codon. There, the first tRNA and the large ribosomal subunit join it. The first tRNA drops off its aminoacid, breaks off and leaves to pick up another amino acid.

The second moves over to make room for another tRNA.

They form a chain of amino acids linked by peptide bonds. When the ribosome reaches a stop codon, it releases the finished polypeptide. Centriole disengagement. The tight link between mother and daughtercentrioles is severed. The centrioles are still connectedby a loose fibrous structure. Centrosome duplication. The mother and daughter centrioles duplicatethemselves—new centrioles form near their proximal ends.

This takes place during S-phase, at the same time as when the cell duplicates its DNA.

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Centriole engagement. The newly formed centrioles reach fulllength. Meanwhile, the original daughtercentriole becomes a mother centriole,and the link between the two is severed.