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Internal Receptors

Internal Receptors

Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.

Short-distance Transport of Resources

Short-distance Transport of Resources

Short-distance transport refers to transport that occurs over a distance of just 2-3 cells, crossing the plasma membrane in the process. Small uncharged molecules, such as oxygen, carbon dioxide, and water, can diffuse across the plasma membrane on their own. In contrast, ions and larger molecules require the assistance of transport proteins due to their charge or size. Transport across membranes also occurs within individual cells, playing a variety of essential roles for the plant as a whole.

Riboswitches

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...

Channel Rhodopsins

Channel Rhodopsins

Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...

Cell Signaling in Plants

Cell Signaling in Plants

Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...

G-Protein Gated Ion Channels

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision. The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...

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Conocimiento estructural de la percepción de los brassinosteroides por BRI1

Ji She¹, Zhifu Han, Tae-Wuk Kim

¹Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University, Beijing 100084, China.

|June 14, 2011

Resumen

Este resumen es generado por máquina.

Las hormonas vegetales llamadas brassinosteroides son clave para el crecimiento. Los investigadores descubrieron cómo el receptor BRI1 reconoce brassinolide a través del análisis estructural, revelando la base molecular para la señalización de la hormona vegetal.

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Área de la Ciencia:

Biología Vegetal Biología Vegetal
Biología Molecular Biología Molecular
La bioquímica es la bioquímica.

Sus antecedentes:

Los brassinosteroides son hormonas vegetales esenciales que regulan el crecimiento y el desarrollo.
La percepción de las hormonas involucra el complejo receptor BRASSINOSTEROID-INSENSITIVE 1 (BRI1).
BRI1 reconoce los brassinosteroides a través de su dominio de repetición extracelular rico en leucina (LRR), iniciando cascadas de señalización.

Objetivo del estudio:

Para aclarar el mecanismo molecular del reconocimiento de brassinosteroides por BRI1.1.
Determinar las estructuras cristalinas del dominio BRI1 LRR en sus estados libre y ligando.
Proporcionar conocimientos estructurales sobre la activación del receptor inducida por brassinosteroides.

Principales métodos:

Se utilizó la cristalografía de rayos X para determinar las estructuras de BRI1 (LRR).
Análisis estructural de BRI1 (LRR) en ambas formas apo y brassinolide-ligado.
Análisis bioquímicos para confirmar el estado monomérico y la unión al ligando.

Principales resultados:

BRI1 ((LRR) funciona como un monómero, independiente de la unión con el brassinolide.
La estructura revela un solenoide helicoidal con un dominio de inserción, formando una ranura de unión.
Brassinolide se une dentro de esta ranura a través de un mecanismo de ajuste inducido, estabilizando los bucles interdominio.

Conclusiones:

El estudio define la base estructural para el reconocimiento de brassinosteroides por el receptor BRI1.
Un mecanismo de ajuste inducido que implica la estabilización del bucle facilita la unión hormonal.
Estos hallazgos ofrecen información crucial sobre los pasos iniciales de la señalización de brassinosteroides y la activación de los receptores.