Video Experimental Relacionado
Updated: May 3, 2026

09:22
Monitoring Immune Cells Trafficking Fluorescent Prion Rods Hours after Intraperitoneal Infection
Published on: November 20, 2010
11.1K
Un gen celular codifica la proteína PrP 27-30 de la tembladera
Cell
|April 1, 1985
Resumen
Los investigadores identificaron la principal proteína en el agente del scrapie, PrP 27-30, de cerebros de hámster infectados. Esta proteína está codificada por un solo gen en los mamíferos, y no es transportada por las partículas infecciosas de la tembladera en sí mismas.
Área de la Ciencia:
- La neurociencia es la neurociencia.
- Biología Molecular Biología Molecular
- Genética La genética.
Sus antecedentes:
- La tembladera es una encefalopatía espongiforme transmisible.
- La proteína principal en las preparaciones purificadas de agentes del scrapie es PrP 27-30.
- El origen y la base genética de PrP 27-30 no se comprendieron completamente.
Objetivo del estudio:
- Para clonar el gen que codifica PrP 27-30.
- Para investigar la base genética de PrP 27-30 en cerebros normales y infectados con scrapie.
- Para determinar si PrP 27-30 está codificado por ácidos nucleicos dentro de los priones de la tembladera.
Principales métodos:
- Las sondas de oligonucleótidos y el cribado de la biblioteca de ADNc para clonar PrP 27-30.
- Southern blotting para analizar el gen PrP.
- análisis de ARNm y Western blotting con antiserum específico.
- La digestión de la proteinasa K para diferenciar las formas de PrP.
Principales resultados:
- Se aisló un clon que codificaba PrP 27-30 del cerebro de un hámster infectado por la tembladera.
- El Southern blotting reveló un solo gen PrP en el ADN normal y infectado de hámster, ratón y humano.
- El ARNm relacionado con PrP estaba presente en niveles similares en cerebros normales e infectados y otros tejidos.
- Se detectó una proteína relacionada con PrP tanto en extractos cerebrales normales como infectados, pero solo PrP 27-30 resistió la digestión de la Proteinasa K en el cerebro infectado.
- No se encontraron ácidos nucleicos relacionados con PrP en priones purificados de la tembladera.
Conclusiones:
- PrP 27-30 está codificado por un solo gen huésped.
- El gen PrP se conserva en todas las especies de mamíferos.
- PrP 27-30 es una proteína huésped, no codificada por el ácido nucleico del agente del scrapie.
Videos de Conceptos Relacionados
Amyloid Fibrils
10.2K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
10.2K
Leaky Scanning
4.5K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R...
4.5K
Signal Sequences and Sorting Receptors
9.9K
Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
9.9K
ER Retrieval Pathway
3.8K
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
3.8K
Directing Proteins to the Rough Endoplasmic Reticulum
12.0K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
12.0K
Subviral Agents
933
Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
933

