Name: catalytic rna: ribozymes in action
Uploaded: 2023-04-30T18:28:42.000Z
Duration: 2 min 47 s
Channel: JoVE

K12 Standards

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NC K-12 Science Standard Course of Study

9-12

Biology

from-molecules-to-organisms-structures-and-processes

From Molecules to Organisms- Structures and Processes

LS.Bio.1.2

Ribozymes

리보자임(Ribozymes)은 효소로 작용할 수 있는 특별한 유형의 RNA입니다. 
대부분의 자연적으로 발생하는 리보자임의 기질은 RNA 포스포디에스테르 결합입니다. 이에 대한 유일하게 알려진 예외는 펩타이드 결합 형성을 촉매하는 박테리아 리보솜의 23S 리보솜 RNA입니다.
리보자임은 모든 유형의 유기체에서 발견되었으며 둘 다 반응 속도를 증가시킨다는 점에서 단백질 기반 효소와 유사합니다. 많은 리보자임은 반응을 촉매하기 위한 보조 인자로 마그네슘과 같은 금속 이온을 필요로 합니다.
일부 종류의 인트론은 리보자임으로 작용할 수 있습니다. 인트론은 핵 mRNA, 핵 tRNA, 고세균, 1족 및 2족 인트론의 5가지 클래스로 분류됩니다.
1족과 2족 인트론은 수백 뉴클레오티드 길이의 큰 리보자임으로, 곰팡이 및 식물 미토콘드리아, 엽록체, 박테리오파지, 진핵생물 바이러스에서 발견됩니다. 
그들은 단백질의 도움 없이 자체 접합할 수 있는 반면, 핵 인트론은 RNA 및 단백질 함유 효소 복합체인 스플라이소솜에 의해 접합됩니다. 
작은 리보자임은 일반적으로 50-150 뉴클레오티드 길이이며 자체 절단 뉴클레오티드 서열 모티프입니다. 이들은 많은 RNA 식물 바이러스와 인간 병원체인 델타 간염 바이러스에서 발견될 수 있습니다. 
이러한 바이러스의 복제 과정은 바이러스 게놈의 여러 단위를 운반하는 긴 RNA를 생성하며, 각 단위는 귀상어와 같은 작은 리보자임을 운반합니다. 이 규칙적인 간격의 귀상어 효소는 자체 절단을 거쳐 긴 RNA가 개별 게놈 분절로 파손됩니다.
대부분의 리보자임은 자신의 뉴클레오티드 염기서열을 절단하지만, 리보뉴클레아제 P는 다른 RNA 분자를 절단할 수 있습니다. 리보뉴클레아제 P는 일부 박테리아에서 발견되며 전구체 tRNA를 처리하여 성숙한 5' 말단을 생성합니다.
자연적으로 이용 가능한 리보자임은 핵산의 인산화 전달 및 단백질의 펩타이드 결합 형성과 같은 좁은 범위의 반응을 촉매하는 것으로 알려져 있습니다. 과학자들은 실험실에서 탄소-탄소 결합 형성 및 산화-환원 반응과 같은 광범위한 반응을 수행할 수 있는 인공 리보자임을 합성했습니다.

<ol>
	<li>도허티, 엘리자베스 A., 제니퍼 A. 다우드나. "리보자임 구조 및 메커니즘." 생물물리학 및 생체 분자 구조 연례 검토 30, no. 1 (2001): 457-475.</li>
	<li>와인버그, 크리스티나 E., 자샤 와인버그, 크리스티안 함만. "새로운 리보자임: 발견, 촉매 메커니즘 및 생물학적 기능을 이해하기 위한 탐구." 핵산 연구 47, no. 18 (2019): 9480-9494. </li>
	<li>Ferré-D'Amaré, Adrian R. 및 William G. Scott. "작은 자체 절단 리보자임." Cold Spring Harbor Perspectives in Biology 2, no. 10 (2010): a003574.</li>
	<li>태너, N. 카일. "리보자임: 촉매 RNA의 특성과 특성." FEMS Microbiology Reviews 23, no. 3 (1999): 257-275.</li>
</ol>

리보자임(ribozymes)

리보자임이라는 용어는 효소로 작용할 수 있는 RNA를 가리키는 데 사용됩니다. 리보자임은 선택된 바이러스, 박테리아, 식물 소기관 및 하급 진핵생물에서 주로 발견됩니다. 리보자임은 1982년 Tom Cech의 실험실에서 그룹 I 인트론이 효소로 작용하는 것을 관찰하면서 처음 발견되었습니다. 이는 Sid Altman의 연구실에서 또 다른 리보자임인 리보뉴클레이스 P를 발견한 이후에 이루어졌습니다. 체흐와 알트만은 둘 다 리보자임에 대한 연구로 1989년에 노벨 화학상을 받았습니다.

리보자임은 크기에 따라 크고 작은 두 그룹으로 분류될 수 있습니다. 큰 리보자임은 크기가 수백에서 수천 개의 뉴클레오티드까지 다양할 수 있습니다. 유형 I 및 II 인트론과 세균성 리보뉴클레이스 P는 큰 리보자임입니다. 작은 리보자임의 길이는 30~150개 뉴클레오티드입니다. 이는 많은 병원성 식물 바이러스와 인간 병원체인 델타 간염 바이러스(HDV)에서 발견됩니다. 귀상어, 머리핀, HDV 및 Varkud 위성은 일반적인 유형의 작은 리보자임입니다. 대부분의 큰 리보자임은 활동을 위해 금속 이온, 특히 Mg2+가 필요하지만 대부분의 작은 리보자임에는 금속 이온이 필요하지 않습니다. glmS mRNA에 있는 glmS 리보자임은 글루코사민 6-포스페이트가 고농도로 존재할 때 리보스위치 역할도 하기 때문에 독특한 a-리보자임입니다.

대부분의 자연 발생 리보자임은 자신의 RNA에 존재하는 포스포디에스테르 결합을 파괴하는 자가 절단을 촉매합니다. 일반적인 단백질 효소와 달리 대부분의 리보자임은 자가 절단 후에는 더 이상 활성이 아니기 때문에 단일 전환 반응을 수행합니다. 그러나 두 개의 리보자임(리보뉴클레이스 P 및 50S 리보솜 하위 단위의 23S RNA)은 서로 다른 반응을 수행합니다. 세균성 리보뉴클레이스 P는 엔도뉴클레아제 활성을 가지며 Mg2+ 이온이 필요한 RNA-단백질 복합체입니다. 그 RNA 구성요소는 미성숙 tRNA의 5' 말단에 작용하여 성숙한 5' 말단을 생성합니다. 리보솜에 존재하는 23S RNA는 인산 전달 반응 대신 번역 중에 펩타이드 결합 형성 반응을 수행한다는 점에서 알려진 다른 모든 천연 리보자임과 다릅니다.

RNA는 효소뿐만 아니라 유전 정보의 전달자 역할을 할 수 있기 때문에, 과거에 RNA가 초기 생명체의 발달에 중요한 역할을 했던 "RNA 세계"가 존재했을 수도 있다는 가설이 세워졌습니다. 그러나 복잡한 생명체가 진화하면서 20개의 아미노산을 가진 단백질이 효소로 작용하기 시작했고 리보자임이 수행하는 많은 반응을 대신했을 수도 있습니다. 이 이론은 아미드 결합 형성, 글리코시드 결합 형성, 탄소-탄소 결합 형성 및 산화-환원 반응과 같은 수많은 반응을 수행할 수 있는 시험관 내에서 개발된 인공 리보자임으로부터 뒷받침됩니다.

리보자임(Ribozymes)

리보자임이라는 용어는 효소로 작용할 수 있는 RNA에 사용됩니다. Ribozymes는 주로 선택된 바이러스, 박테리아, 식물 세포 기관에서 발견되며 ...

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Cell Biology

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Energy and Catalysis

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KEY TERMS AND CONCEPTS

주요 용어 및 개념

catalytic rna: ribozymes in action

Ribozymes are RNA molecules that can act as enzymes. They help speed up specific chemical reactions without being protein enzymes. This makes them an important example of RNA with more than one job in the cell.

Some ribozymes can cut RNA molecules, and others can join them together. This shows that RNA can do catalytic work as well as carry genetic information. Ribozymes are a key part of how scientists think about the many roles of RNA in biology.

One well-known ribozyme is ribonuclease P, or RNase P. It helps process precursor tRNA into mature tRNA by removing extra RNA at one end. This process is important because tRNA must be correctly trimmed before it can function in protein synthesis.

Catalytic RNA: Ribozymes in Action

the first law of thermodynamics

Energy Changes in Cells and Matter

The first law of thermodynamics describes how energy changes form in the universe. The total amount of energy stays constant. Energy can move from one place to another or change into a different form, but it cannot be created or destroyed. These energy changes happen in everyday life. A light bulb changes electrical energy into light energy. A gas stove changes chemical energy in natural gas into heat energy. Plants also carry out a major energy transformation when they convert sunlight energy...

the second law of thermodynamics

Entropy and Spontaneous Change

Entropy helps predict whether a process will happen on its own. Entropy is a measure of randomness or disorder in a system. High entropy means high disorder and low energy. A student’s bedroom is a simple example. If no work is done, the room becomes messy over time. That messy state is highly disordered and has high entropy. To make the room clean again, energy must be added as the student puts things away. That organized state has low entropy. Processes that increase the entropy of the...

enthalpy within the cell

Cellular Enthalpy and Energy Changes

Cellular enthalpy describes how heat and energy change during chemical and physical processes. Enthalpy is written as H and is defined as the sum of a system’s internal energy, U, and the product of pressure and volume, PV. It is a state function, which means its value depends on the state of the system, not the path taken. Scientists cannot measure the enthalpy of a single substance directly. They can determine enthalpy changes, or ΔH, for a process instead. For reactions or changes that...

entropy within the cell

Cell Energy Loss and Entropy

Cell energy loss and entropy explain why living things need constant energy input. Cells obtain energy, transform it, and use it to do work, but these transfers are never completely efficient. In each transfer, some energy is lost in a form that cannot be used. In many cases, that lost energy is heat energy.

an introduction to free energy

Gibbs Free Energy and Reaction Work

Gibbs free energy describes the usable energy in a chemical reaction. It helps scientists compare how much energy different reactions release. This measurement is called Gibbs free energy, or G, after Josiah Willard Gibbs. The second law of thermodynamics explains why not all energy stays available for work. Some energy is lost in an unusable form, such as heat, and this loss increases entropy. Gibbs free energy is the energy left after that entropy loss is taken into account. Every chemical...

endergonic and exergonic reactions in the cell

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Cell Reactions That Release or Store Energy

Cell reactions can either release energy or store it for later use. In chemistry, this difference is described by the value of ΔG, or free energy change. When energy is released during a reaction, ΔG is negative. The products then have less free energy than the reactants because some free energy has been given off. Reactions with a negative ΔG are called exergonic reactions. Exergonic means energy is leaving the system. These reactions are also called spontaneous reactions because they can...

the equilibrium binding constant and binding strength

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How Equilibrium Binding Constant Affects Binding

The equilibrium binding constant describes how strongly two molecules bind at equilibrium. It is a useful way to compare binding strength in molecular interactions. This topic focuses on how binding is measured and what the equilibrium binding constant means. A higher value indicates stronger binding, while a lower value indicates weaker binding. Understanding this constant helps explain how tightly molecules stay together under equilibrium conditions. The page also connects the binding...

free energy and equilibrium

Free Energy and Reaction Direction

Free energy and reaction direction are linked in chemical equilibrium. A free energy change, ΔG, shows the driving force for a process. When ΔG is negative, the process is driven forward. When ΔG is positive, the reverse direction is favored. When ΔG is zero, the forward and reverse driving forces are equal, and the system is at equilibrium. The reaction quotient, Q, helps show how close a system is to equilibrium. Q is the numerical value of the mass action expression for the system. It can...

non-equilibrium in the cell

Cells Stay Out of Equilibrium

Cells stay out of chemical equilibrium by constantly using energy and moving materials in and out. Chemical reactions in metabolism are often reversible. They can go in both directions. In one direction, they release energy to the surroundings. In the reverse direction, they absorb energy. The same idea applies to reactions that build and break down cell molecules. Proteins, for example, can be broken into individual amino acids, and amino acids can be used to build proteins again. In a closed...

oxidation and reduction of organic molecules

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Electron Carriers in Cell Energy Transfer

Cell energy production depends on redox reactions, which are oxidation and reduction reactions that happen together. In oxidation, an electron is removed from an atom in a compound. In reduction, that same electron is added to another compound. Because these reactions usually occur as a pair, they are called redox reactions. When a molecule loses an electron, its potential energy goes down. The electron does not stay free in the cytoplasm. Instead, it moves to a second compound and reduces...

introduction to enzymes

Enzyme Function, Cofactors, and Inhibitors

Enzymes are proteins that speed up biochemical reactions without being used up. Humans have used enzymes since about 7000 BCE, when they fermented sugars to make alcohol without knowing the reaction was enzyme-catalyzed. The word enzyme was coined by Wilhelm Kuhne in 1877. It comes from the Greek words en, meaning “in” or “within,” and zyme, meaning “yeast.” Enzymes work through active sites, which are regions that bind substrates and help convert them into products. Many enzymes also have...

enzymes and activation energy

How Enzymes Lower Reaction Energy

Enzymes lower the energy needed for a chemical reaction to begin. That starting energy is called activation energy, or free energy of activation, and it is often written as Ea. During a reaction, bonds break and new bonds form. In glucose breakdown, for example, bonds between carbon atoms break and release energy because they are energy-storing bonds. Before a reaction can move forward, reactant molecules must reach a high-energy, unstable shape called the transition state. To get there, the...

introduction to enzyme kinetics

Graphing Enzyme Kinetics Data

Enzyme kinetics uses graphs to show how fast a biochemical reaction happens. Scientists measure the initial reaction rate, or velocity (Vo), at different substrate concentrations ([S]). They may also run trials with inhibitors or other molecules that change the reaction rate. The results are often plotted as Vo against [S]. For many single-substrate reactions, the data fits the Michaelis-Menten equation. This equation, named after Leonor Michaelis and Maud Menten, helps estimate the maximum...

turnover number and catalytic efficiency

How Fast Enzymes Work in Digestion

Enzymes can work at very different speeds, and their turnover number shows how fast they convert substrate molecules into products. Turnover number is the maximum number of substrate molecules an enzyme can transform per unit time. For most enzymes, this value is between 1 and 1000 molecules per second. Some enzymes are especially fast. Catalase has the highest known turnover number and can convert up to 2.8×10^6 molecules of hydrogen peroxide into water and oxygen each second. Lysozyme has...

catalytically perfect enzymes

Diffusion-Controlled Enzymes and Reaction Speed

Catalytically perfect enzymes are enzymes that speed up biochemical reactions at very high rates. The idea was first proposed by W. J. Albery and J. R. Knowles in 1976. These enzymes have catalytic efficiency values of about 10^8 to 10^9 M^-1 s^-1 and are also called diffusion-controlled enzymes because diffusion of the substrate into the active site is the only rate-limiting step. Examples of catalytically perfect enzymes include triose phosphate isomerase, fumarase, and superoxide dismutase.

introduction to mechanisms of enzyme catalysis

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How Enzymes Change Shape to Catalyze

Enzyme catalysis depends on how enzymes bind substrates and how the active site responds during the reaction. Scientists once described this process with a simple lock-and-key model, where the enzyme and substrate fit together in one instant. Research now supports induced fit, a more dynamic model in which binding causes a small change in the enzyme’s shape. That shift helps create an ideal match between the enzyme and the substrate’s transition state, which improves catalysis. The active site...

ligand binding and linkage

Ligand Binding and Allosteric Effects

Ligand binding and linkage describe how one molecule can affect another when it binds to a protein. In this topic, the focus is on how binding at one site can influence activity at a different site on the same protein. This idea is important for understanding protein function in high school biology. It helps explain why some proteins respond more strongly after a ligand attaches. The transcript centers on the connection between ligand binding and linkage, which is a key concept in molecular...

cooperative allosteric transitions

How Proteins Shift Shape Together

Proteins can change shape in a coordinated way during allosteric transitions. In a cooperative transition, one part of the protein affects another part, so the change spreads through the molecule. These shape changes help proteins switch between different states. The shift can influence how the protein works and how it responds to other molecules. Cooperative allosteric transitions are an important idea in protein function. They explain how a small change at one site can lead to a larger...

ribozymes

Ribozymes are RNA molecules that can act as enzymes. They help speed up specific chemical reactions without being protein enzymes. This makes them an important example of RNA with more than one job in the cell. Some ribozymes can cut RNA molecules, and others can join them together. This shows that RNA can do catalytic work as well as carry genetic information. Ribozymes are a key part of how scientists think about the many roles of RNA in biology. One well-known ribozyme is ribonuclease P,...

atp energy storage and release

ATP Powers Cellular Transport and Reactions

ATP powers cellular transport and many reactions by transferring energy through phosphorylation. ATP is a highly unstable molecule. If it is not used quickly, it breaks down into ADP and inorganic phosphate, and the released energy is lost as heat. Cells use ATP through energy coupling. This means the exergonic reaction of ATP hydrolysis is linked to an endergonic reaction so the reaction can move forward. One major example is the sodium-potassium pump, a transmembrane ion pump that is vital...

atp and macromolecule synthesis

ATP in Building Cell Macromolecules

ATP helps cells build biological macromolecules. These organic compounds are mainly made of carbon atoms bonded to hydrogen, oxygen, nitrogen, and small amounts of other elements. The four major classes of biological macromolecules are carbohydrates, lipids, proteins, and nucleic acids. Most macromolecules start as small subunits called monomers. Cells join monomers with covalent bonds to make larger molecules called polymers. This building process needs energy, so cells depend on ATP, the...

coupled reactions

ATP Powers Cellular Work

ATP powers many kinds of cellular work by coupling energy-releasing reactions to energy-requiring ones. Some reactions happen on their own and release energy. Others need an energy input to move forward. Cells link these reactions so important processes can still occur. Adenosine triphosphate, or ATP, stores energy that cells can use quickly. ATP hydrolysis is the breaking of ATP, and it releases energy. Cells often use that released energy to drive endergonic reactions, which are reactions...

key terms and concepts

Explore ribozymes, RNA molecules that act as enzymes, cut or join RNA, and help process precursor tRNA into mature tRNA for protein synthesis.

Catalytic RNA: Ribozymes in Action | JoVE K12

cell biology

JoVE Core Cell Biology illustrates complex cellular processes in easy-to-understand yet comprehensive animated video lessons. This collection focuses on the essential components and functions of cells, including organelles and membranes, cellular transport, and cell energetics. It is complemented by scientist-in-action videos that demonstrate the application of cell biology in real-world research experiments.

Virginia  Standards of Learning

HIgh School

BIO.2

BIO.2.c

Florida Department of Education

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Life Science

SC.912.L.18

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SC.912.L.18.11

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BIO.11

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Compounds Essential to Human Function

The human body is composed of cells that are fundamentally made up of several different molecules. These molecules are essential to carry out all ...

Macromolecules

Biomolecules
Organisms contain a wide variety of organic molecules with numerous functions which depend on the chemical structures and properties of these ...

Solution Preparation
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Identifying Macromolecules with Indicator Solutions
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pH Regulation in Cells

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Chemistry of the Cell

Overview of Functional Groups

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Introduction to Carbohydrates

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Carbohydrate Metabolism

Sugars as Energy Storage Molecules

What are Lipids?

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Lipid-derived Compounds in the Human Body

Fats and lipids are crucial components in the human body. Some lipid-derived compounds, such as fat-soluble vitamins, eicosanoids, lipoproteins, and ...

Fats as Energy Storage Molecules

What are Proteins?

Protein Organization

Globular Proteins

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Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of ...

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. ...

Role of Proteins in the Human Body

Proteins are the building block of life. They are also&#160; the most abundant macromolecules with as many diverse roles in the body. They are part of ...

Nucleic Acids and Nucleotides

Nucleic acids are the most important macromolecules for the continuity of life. They carry the cell&#39;s genetic blueprint and have instructions for its ...

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group ...

ATP Energy Storage and Release

ATP and Macromolecule Synthesis

Biological macromolecules are organic compounds, predominantly composed of carbon atoms. The carbon atoms are covalently bonded with hydrogen, oxygen, ...

Construct an explanation to illustrate relationships between structure and function of major macromolecules essential for life.

LS.Bio.1.1

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an ...

Enzymes and Activation Energy

The activation energy (or free energy of activation), abbreviated as Ea, is the small amount of energy input necessary for all chemical reactions to ...

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate ...

Turnover Number and Catalytic Efficiency

The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from ...

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at ...

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple &#34;lock-and-key&#34; fashion. This model stated that the enzyme ...

Ligand Binding and Linkage

Cooperative Allosteric Transitions

Carry out investigations to illustrate how enzymes act as catalysts for biochemical reactions and how environmental factors affect enzyme activity.

What are Cells?

Cells are the smallest and basic units of life, whether it is a single cell that forms the entire organism, e.g., in a bacterium or trillions of them, ...

Cell Size

Cell sizes vary widely among and within organisms. Bacterial cells range between 1-10 micrometers (&#x3BC;m)and are considerably smaller than most ...

Eukaryotic Compartmentalization

One of the distinguishing features of eukaryotic cells is that they contain membrane-bound organelles, such as the nucleus and mitochondria, that carry ...

Prokaryotic Cells

Prokaryotes are small unicellular organisms that include the domains&#x2014;Archaea and Bacteria. Bacteria include many common organisms, such as ...

Cytoplasm

The cytoplasm consists of organelles and a framework of protein scaffolds called the cytoskeleton suspended in an aqueous solution, the cytosol. The ...

The Nucleus

The nucleus is a membrane-bound organelle that acts as a control center in a eukaryotic cell. It contains chromosomal DNA, which controls gene expression ...

Endoplasmic Reticulum

Endoplasmic ReticulumThe endoplasmic reticulum (ER) is an extensive network of membranous sacs and tubules in eukaryotic cells, continuous with the outer ...

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that ...

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are ...

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules ...

Peroxisomes

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration&#x2014;the ...

Introduction to the Cytoskeleton

Overview of the Cytoskeleton
The cytoskeleton is a network of protein filaments present within the cell, having three distinct filaments ...

Introduction to Actin

Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle ...

Cell Structure

Background
Cells represent the most basic biological units of all organisms, whether it be simple, single-celled organisms like bacteria, or large, ...

overview-of-myosin-structure-and-function

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with ...

Use models to explain how the structure of organelles determines its function and supports overall cell processes.

LS.Bio.1.3

Analyze how the relationship between structure and function supports life processes within organisms.

Catalytic RNA: Ribozymes in Action

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