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Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
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Translation01:31

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Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of...
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Initiation of Translation02:33

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome...
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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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Un solo interruptor de aminoácidos altera la especificidad del donante de isopreno en las peniltransferasas

Paola Estrada, Maho Morita1, Yue Hao

  • 1Department of Medicinal Chemistry , University of Utah , Salt Lake City , Utah 84112 , United States.

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Resumen
Este resumen es generado por máquina.

Una sola mutación de aminoácido puede cambiar la especificidad de la preniltransferasa entre los donantes de isopreno C5 y C10. Este descubrimiento permite la modificación precisa de lípidos de los productos naturales de péptidos para aplicaciones de biología sintética.

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Área de la Ciencia:

  • La bioquímica
  • Biología sintética
  • Productos naturales Química

Sus antecedentes:

  • Las preniltransferasas modifican los péptidos (RiPP) utilizando donantes de isopreno C5.
  • Se identificó una nueva modificación de O-geranilo en Tyr en la piriclamida 70005E1.

Objetivo del estudio:

  • Investigar el mecanismo de una nueva preniltransferasa C10 (PirF).
  • Para determinar si la especificidad del donante de la preniltransferasa puede ser manipulada.

Principales métodos:

  • Reconstitución enzimática y estudios cinéticos del PirF.
  • Cristalografía de rayos X del PirF.
  • Mutagénesis dirigida al sitio de las preniltransferasas.

Principales resultados:

  • PirF utiliza un donante de geranilo C10 y no un donante de dimetilalillo C5.
  • Un solo cambio de aminoácido cerca del sitio activo dicta la especificidad del donante C5 vs C10.
  • Las enzimas de ingeniería pueden unir lípidos C5 o C10 a los antipéptidos.

Conclusiones:

  • La especificidad del donante de la preniltransferasa es altamente sintonizable a través de mutaciones de un solo aminoácido.
  • Esto proporciona una herramienta poderosa para la biología sintética para modificar los productos naturales de péptidos.