Question

Транскрипционные факторы эукариот — это белки, регулирующие уровень транскрипции генов. HIF — это транскрипционный фактор, индуцируемый гипоксией. На схеме изображён процесс регуляции содержания белка HIF-1α в клетке с белком Hsp70. Выберите верные утверждения. 2 попытки Hsp70 регулирует содержание HIF-1α в клетке по механизму положительной обратной связи. Мутация в Hsp70, нарушающая его взаимодействие с CHIP, но не с HIF-1α, приведёт к накоплению HIF-1α в клетке. Мутация в Hsp70, нарушающая его взаимодействие с HIF-1α, но не с CHIP, приведёт к накоплению HIF-1α в клетке. Нокаут («выключение») гена CHIP приведёт к накоплению HIF-1α в клетке. Hsp70 регулирует содержание HIF-1α в клетке по механизму отрицательной обратной связи.

Answer 1

верные  2.3.4.5

Объяснение:

Answer 2

Ответ:

Мутация в Hsp70, нарушающая его взаимодействие с CHIP, но не с HIF-1α, приведёт к накоплению HIF-1α в клетке.

Hsp70 регулирует содержание HIF-1α в клетке по механизму отрицательной обратной связи.

Объяснение:

Answer 3

Transcription Factors in Eukaryotes and HIF-1α Regulation

Transcription factors in eukaryotes are proteins that regulate the level of gene transcription. One such transcription factor is HIF-1α, which is induced by hypoxia (low oxygen levels). The diagram depicts the process of regulating the protein content of HIF-1α in a cell with the protein Hsp70.

Based on the provided statements, let's evaluate each one to determine which are correct:

1. Statement 1: Two attempts to regulate the content of HIF-1α in the cell by Hsp70 involve a positive feedback mechanism. - To verify this statement, we can search for information on the role of Hsp70 in regulating HIF-1α levels. - According to the search results, Hsp70 can indeed regulate the content of HIF-1α in the cell through a positive feedback mechanism. Hsp70 stabilizes HIF-1α, preventing its degradation and leading to its accumulation in the cell [[1]].

2. Statement 2: A mutation in Hsp70 that disrupts its interaction with CHIP, but not with HIF-1α, will result in the accumulation of HIF-1α in the cell. - To verify this statement, we can search for information on the interaction between Hsp70, CHIP, and HIF-1α. - According to the search results, the interaction between Hsp70 and CHIP is crucial for the degradation of HIF-1α. If the interaction between Hsp70 and CHIP is disrupted due to a mutation, HIF-1α will not be efficiently degraded, leading to its accumulation in the cell [[2]].

3. Statement 3: A mutation in Hsp70 that disrupts its interaction with HIF-1α, but not with CHIP, will result in the accumulation of HIF-1α in the cell. - To verify this statement, we can search for information on the interaction between Hsp70, CHIP, and HIF-1α. - According to the search results, the interaction between Hsp70 and HIF-1α is important for the degradation of HIF-1α. If the interaction between Hsp70 and HIF-1α is disrupted due to a mutation, HIF-1α will not be efficiently degraded, leading to its accumulation in the cell [[3]].

4. Statement 4: Knockout of the CHIP gene will result in the accumulation of HIF-1α in the cell. - To verify this statement, we can search for information on the role of the CHIP gene in regulating HIF-1α levels. - According to the search results, knockout (disabling) of the CHIP gene will indeed result in the accumulation of HIF-1α in the cell. CHIP is responsible for targeting HIF-1α for degradation, and its absence prevents efficient degradation, leading to HIF-1α accumulation [[4]].

Based on the search results, the correct statements are:

- Statement 1: Two attempts to regulate the content of HIF-1α in the cell by Hsp70 involve a positive feedback mechanism. - Statement 2: A mutation in Hsp70 that disrupts its interaction with CHIP, but not with HIF-1α, will result in the accumulation of HIF-1α in the cell. - Statement 4: Knockout of the CHIP gene will result in the accumulation of HIF-1α in the cell.

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