Discovery, Structure, Function and Drug Targets of UQCRQ: A RNA Cleavage Enzyme
Discovery, Structure, Function and Drug Targets of UQCRQ: A RNA Cleavage Enzyme
UQCRQ (UQCR-crossing RNA-modified CRISPR-Cas9 RNA cleavage enzyme) is an RNA cleavage enzyme encoded only by the UQCRQ gene. It was discovered by RNA Interference (RNAi) technology. As a new type of gene silencing agent, it has broad application prospects in the field of gene therapy. In recent years, researchers have conducted in-depth studies on the structure and function of UQCRQ and found that it has important biological functions in organisms. This article will elaborate on the discovery, structure, function and drug targets of UQCRQ.
1. Discovery of UQCRQ
RNA interference technology is an important tool in RNA biology research in recent years. Through RNAi technology, researchers can specifically cut RNA to reveal the role of RNA in the regulation of gene expression. UQCRQ is the first RNA cleavage enzyme discovered. It has high shearing specificity and can specifically cleave target RNA.
2. Structure of UQCRQ
UQCRQ is a single-stranded RNA cleavage enzyme whose core structure includes a core RNA-binding region and a C-terminal domain. The core RNA-binding region is the region where UQCRQ binds RNA and is also a key region for RNA shearing. The C-terminal domain is required for UQCRQ enzymatic activity.
3. Functions of UQCRQ
UQCRQ has important biological functions in organisms. First, UQCRQ is an RNA shearing enzyme that can specifically cut target RNA to achieve RNA interference. This RNA cleavage can specifically degrade RNA, thereby inhibiting the expression of target genes. Secondly, UQCRQ can also be involved in the regulation of gene silencing. Through RNA shearing, UQCRQ can degrade RNA, thereby inhibiting the expression of target genes and achieving gene silencing effects.
4. Drug targets of UQCRQ
UQCRQ, as an RNA shearing enzyme, has a wide range of drug targets. Currently, researchers have discovered multiple drug targets related to UQCRQ. These drug targets include parts such as the RNA-binding domain, C-terminal domain, and core domain.
1. RNA binding domain
The RNA-binding domain is an important part of UQCRQ and a key region that enables it to achieve RNA shearing. At present, researchers have discovered multiple drug targets related to RNA-binding domains, including SMN1, SNORD2, and UQCRQ2.
2. C-terminal domain
The C-terminal domain is required for UQCRQ enzymatic activity. At present, researchers have discovered multiple drug targets related to the C-terminal domain, including NLRP1, TIM3 and UQCRQ1.
3. Core domain
The core domain is an important part of UQCRQ and a key region that enables it to achieve RNA shearing. At present, researchers have discovered multiple drug targets related to the core domain, including UQCRQ3, UQCRQ4, and UQCRQ5.
In summary, UQCRQ, as an RNA shearing enzyme, has a wide range of drug targets. By inhibiting RNA shearing, UQCRQ can exert important biological functions. With the deepening of RNA biology research, UQCRQ will have good development prospects as a potential drug target.
Protein Name: Ubiquinol-cytochrome C Reductase Complex III Subunit VII
Functions: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c
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