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Related Concept Videos

Ribozymes02:47

Ribozymes

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
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Restriction Enzymes01:11

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Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
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Base Excision Repair01:54

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One of the common DNA damages is the chemical alteration of single bases by alkylation, oxidation, or deamination. The altered bases cause mispairing and strand breakage during replication. This type of damage causes minimal change to the DNA double helix structure and can be repaired by the base excision repair (BER) pathways. BER corrects damaged DNA sequences by removing the damaged base and restoring the original base sequence using the complementary strand as a template.
The first step of...
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DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
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Author Spotlight: Characterizing Novel Enzymes from Extremophiles and Common Pathogens to Understand DNA Repair and Replication
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Exoribonucleases and Endoribonucleases.

Zhongwei Li, Murray P Deutscher

    Ecosal Plus
    |October 8, 2015
    PubMed
    Summary

    This review details Escherichia coli ribonucleases (RNases), including eight exoribonucleases and seven endoribonucleases. It classifies these enzymes by family, structure, and function, highlighting their roles in RNA processing.

    Area of Science:

    • Molecular Biology
    • Enzymology
    • Microbiology

    Background:

    • Escherichia coli possesses a complex system of ribonucleases (RNases) essential for RNA metabolism.
    • RNases play critical roles in RNA degradation, processing, and quality control within the cell.

    Purpose of the Study:

    • To comprehensively review the known Escherichia coli ribonucleases (RNases).
    • To describe their structures, catalytic properties, genes, physiological roles, and regulation.
    • To categorize RNases into families based on sequence and function.

    Main Methods:

    • Review of existing literature on E. coli RNases.
    • Analysis of sequence data and catalytic properties.
    • Classification of exoribonucleases into four families (RNR, DEDD, RBN, PDX).

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  • Identification and characterization of seven well-known endoribonucleases.

    • Main Results:

    • Eight exoribonucleases (RNases II, R, D, T, PH, BN, polynucleotide phosphorylase (PNPase), and oligoribonuclease (ORNase)) are identified and grouped into four families.
    • Seven endoribonucleases (RNases I, III, P, E, G, HI, and HII) are described, with most requiring divalent cations for activity.
    • RNase H specifically targets the RNA strand in RNA-DNA hybrids and is conserved across organisms.
    • Evidence suggests the existence of additional uncharacterized endoribonucleases in E. coli.

    Conclusions:

    • The characterized RNases in E. coli exhibit diverse structures and functions crucial for RNA homeostasis.
    • The classification into families aids in understanding evolutionary relationships and catalytic mechanisms.
    • Further research is needed to identify and characterize the full spectrum of E. coli endoribonucleases and their roles.