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  1. Book: Ribonuclease P

    Liu, Fenyong

    (Protein reviews ; 10)

    2010  

    Author's details Fenyong Liu ... ed
    Series title Protein reviews ; 10
    Collection
    Language English
    Size XVI, 283 S. : zahlr. Ill.
    Publisher Springer Science+Business Media
    Publishing place New York, NY u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT016035059
    ISBN 978-1-441-91141-4 ; 9781441911421 ; 1-441-91141-3 ; 1441911421
    Database Catalogue ZB MED Medicine, Health

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  2. Article ; Online: The discovery of a catalytic RNA within RNase P and its legacy.

    Kirsebom, Leif A / Liu, Fenyong / McClain, William H

    The Journal of biological chemistry

    2024  , Page(s) 107318

    Abstract: Sidney Altman's discovery of the processing of one RNA by another RNA that acts like an enzyme was revolutionary in biology and the basis for his sharing the 1989 Nobel Prize in Chemistry with Tom Cech. These breakthrough findings support the key role of ...

    Abstract Sidney Altman's discovery of the processing of one RNA by another RNA that acts like an enzyme was revolutionary in biology and the basis for his sharing the 1989 Nobel Prize in Chemistry with Tom Cech. These breakthrough findings support the key role of RNA in molecular evolution, where replicating RNAs (and similar chemical derivatives) either with or without peptides functioned in protocells during the early stages of life on Earth, an era referred to as the RNA world (1,2). Here, we cover the historical background highlighting the work of Altman and his colleagues and the subsequent efforts of other researchers to understand the biological function of RNase P and its catalytic RNA subunit, and to employ it as a tool to downregulate gene expression. We primarily discuss bacterial RNase P-related studies but acknowledge that many groups have significantly contributed to our understanding of archaeal and eukaryotic RNase P, as reviewed in this special issue and elsewhere (3-7).
    Language English
    Publishing date 2024-04-25
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2024.107318
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Human RNase P: overview of a ribonuclease of interrelated molecular networks and gene-targeting systems.

    Jarrous, Nayef / Liu, Fenyong

    RNA (New York, N.Y.)

    2022  Volume 29, Issue 3, Page(s) 300–307

    Abstract: The seminal discovery of ribonuclease P (RNase P) and its catalytic RNA by Sidney Altman has not only revolutionized our understanding of life, but also opened new fields for scientific exploration and investigation. This review focuses on human RNase P ... ...

    Abstract The seminal discovery of ribonuclease P (RNase P) and its catalytic RNA by Sidney Altman has not only revolutionized our understanding of life, but also opened new fields for scientific exploration and investigation. This review focuses on human RNase P and its use as a gene-targeting tool, two topics initiated in Altman's laboratory. We outline early works on human RNase P as a tRNA processing enzyme and comment on its expanding nonconventional functions in molecular networks of transcription, chromatin remodeling, homology-directed repair, and innate immunity. The important implications and insights from these discoveries on the potential use of RNase P as a gene-targeting tool are presented. This multifunctionality calls to a modified structure-function partitioning of domains in human RNase P, as well as its relative ribonucleoprotein, RNase MRP. The role of these two catalysts in innate immunity is of particular interest in molecular evolution, as this dynamic molecular network could have originated and evolved from primordial enzymes and sensors of RNA, including predecessors of these two ribonucleoproteins.
    MeSH term(s) Humans ; Ribonuclease P/genetics ; Ribonuclease P/metabolism ; RNA/genetics ; RNA Processing, Post-Transcriptional ; RNA, Catalytic/metabolism
    Chemical Substances Ribonuclease P (EC 3.1.26.5) ; RNA (63231-63-0) ; RNA, Catalytic
    Language English
    Publishing date 2022-12-22
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1241540-6
    ISSN 1469-9001 ; 1355-8382
    ISSN (online) 1469-9001
    ISSN 1355-8382
    DOI 10.1261/rna.079475.122
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: External Guide Sequence Effectively Suppresses the Gene Expression and Replication of Herpes Simplex Virus 2.

    Yan, Bin / Liu, Yujun / Chen, Yuan-Chuan / Liu, Fenyong

    Molecules (Basel, Switzerland)

    2024  Volume 29, Issue 9

    Abstract: Ribonuclease P (RNase P) complexed with an external guide sequence (EGS) represents a promising nucleic acid-based gene targeting approach for gene expression knock-down and modulation. The RNase P-EGS strategy is unique as an EGS can be designed to ... ...

    Abstract Ribonuclease P (RNase P) complexed with an external guide sequence (EGS) represents a promising nucleic acid-based gene targeting approach for gene expression knock-down and modulation. The RNase P-EGS strategy is unique as an EGS can be designed to basepair any mRNA sequence and recruit intracellular RNase P for hydrolysis of the target mRNA. In this study, we provide the first direct evidence that the RNase P-based approach effectively blocks the gene expression and replication of herpes simplex virus 2 (HSV-2), the causative agent of genital herpes. We constructed EGSs to target the mRNA encoding HSV-2 single-stranded DNA binding protein ICP8, which is essential for viral DNA genome replication and growth. In HSV-2 infected cells expressing a functional EGS, ICP8 levels were reduced by 85%, and viral growth decreased by 3000 folds. On the contrary, ICP8 expression and viral growth exhibited no substantial differences between cells expressing no EGS and those expressing a disabled EGS with mutations precluding RNase P recognition. The anti-ICP8 EGS is specific in targeting ICP8 because it only affects ICP8 expression but does not affect the expression of the other viral immediate-early and early genes examined. This study shows the effective and specific anti-HSV-2 activity of the RNase P-EGS approach and demonstrates the potential of EGS RNAs for anti-HSV-2 applications.
    MeSH term(s) Herpesvirus 2, Human/genetics ; Herpesvirus 2, Human/physiology ; Virus Replication ; Gene Expression Regulation, Viral ; Humans ; Ribonuclease P/metabolism ; Ribonuclease P/genetics ; Animals ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Chlorocebus aethiops ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Vero Cells ; Immediate-Early Proteins/genetics ; Immediate-Early Proteins/metabolism ; DNA-Binding Proteins
    Chemical Substances Ribonuclease P (EC 3.1.26.5) ; Viral Proteins ; ICP8 protein, Simplexvirus ; RNA, Messenger ; Immediate-Early Proteins ; DNA-Binding Proteins
    Language English
    Publishing date 2024-04-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules29092052
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Mapping of RNase P Ribozyme Regions in Proximity with a Human RNase P Subunit Protein Using Fe(II)-EDTA Cleavage and Nuclease Footprint Analyses.

    Trang, Phong / Smith, Adam / Liu, Fenyong

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2666, Page(s) 55–67

    Abstract: Ribonuclease P (RNase P), which may consist of both protein subunits and a catalytic RNA part, is responsible for 5' maturation of tRNA by cleaving the 5'-leader sequence. In Escherichia coli, RNase P contains a catalytic RNA subunit (M1 RNA) and a ... ...

    Abstract Ribonuclease P (RNase P), which may consist of both protein subunits and a catalytic RNA part, is responsible for 5' maturation of tRNA by cleaving the 5'-leader sequence. In Escherichia coli, RNase P contains a catalytic RNA subunit (M1 RNA) and a protein factor (C5 protein). In human cells, RNase P holoenzyme consists of an RNA subunit (H1 RNA) and multiple protein subunits that include human RPP29 protein. M1GS, a sequence specific targeting ribozyme derived from M1 RNA, can be constructed to target a specific mRNA to degrade it in vitro. Recent studies have shown that M1GS ribozymes are efficient in blocking the expression of viral mRNAs in cultured cells and in animals. These results suggest that RNase P ribozymes have the potential to be useful in basic research and in clinical applications. It has been shown that RNase P binding proteins, such as C5 protein and RPP29, can enhance the activities of M1GS RNA in processing a natural tRNA substrate and a target mRNA. Understanding how RPP29 binds to M1GS RNA and enhances the enzyme's catalytic activity will provide great insight into developing more robust gene-targeting ribozymes for in vivo application. In this chapter, we describe the methods of using Fe(II)-ethylenediaminetetraacetic acid (EDTA) cleavage and nuclease footprint analyses to determine the regions of a M1GS ribozyme that are in proximity to RPP29 protein.
    MeSH term(s) Animals ; Humans ; Ribonuclease P/genetics ; Ribonuclease P/metabolism ; RNA, Catalytic/metabolism ; Edetic Acid ; Protein Subunits/metabolism ; RNA/chemistry ; RNA, Messenger/genetics ; Escherichia coli/metabolism ; Endonucleases/metabolism
    Chemical Substances Ribonuclease P (EC 3.1.26.5) ; RNA, Catalytic ; Fe(II)-EDTA (15651-72-6) ; Edetic Acid (9G34HU7RV0) ; Protein Subunits ; RNA (63231-63-0) ; RNA, Messenger ; Endonucleases (EC 3.1.-)
    Language English
    Publishing date 2023-05-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3191-1_4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: A RNase P Ribozyme Inhibits Gene Expression and Replication of Hepatitis B Virus in Cultured Cells.

    Yan, Bin / Liu, Yujun / Chen, Yuan-Chuan / Liu, Fenyong

    Microorganisms

    2023  Volume 11, Issue 3

    Abstract: Hepatitis B virus (HBV), an international public health concern, is a leading viral cause of liver disease, such as hepatocellular carcinoma. Sequence-specific ribozymes derived from ribonuclease P (RNase P) catalytic RNA are being explored for gene ... ...

    Abstract Hepatitis B virus (HBV), an international public health concern, is a leading viral cause of liver disease, such as hepatocellular carcinoma. Sequence-specific ribozymes derived from ribonuclease P (RNase P) catalytic RNA are being explored for gene targeting applications. In this study, we engineered an active RNase P ribozyme, M1-S-A, targeting the overlapping region of HBV S mRNA, pre-S/L mRNA, and pregenomic RNA (pgRNA), all deemed essential for viral infection. Ribozyme M1-S-A cleaved the S mRNA sequence efficiently in vitro. We studied the effect of RNase P ribozyme on HBV gene expression and replication using the human hepatocyte HepG2.2.15 culture model that harbors an HBV genome and supports HBV replication. In these cultured cells, the expression of M1-S-A resulted in a reduction of more than 80% in both HBV RNA and protein levels and an inhibition of about 300-fold in the capsid-associated HBV DNA levels when compared to the cells that did not express any ribozymes. In control experiments, cells expressing an inactive control ribozyme displayed little impact on HBV RNA and protein levels, and on capsid-associated viral DNA levels. Our study signifies that RNase P ribozyme can suppress HBV gene expression and replication, implying the promise of RNase P ribozymes for anti-HBV therapy.
    Language English
    Publishing date 2023-03-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms11030654
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Suppressing Kaposi's Sarcoma-Associated Herpesvirus Lytic Gene Expression and Replication by RNase P Ribozyme.

    Liu, Yujun / Chen, Yuan-Chuan / Yan, Bin / Liu, Fenyong

    Molecules (Basel, Switzerland)

    2023  Volume 28, Issue 8

    Abstract: Kaposi's sarcoma, an AIDS-defining illness, is caused by Kaposi's sarcoma-associated herpesvirus (KSHV), an oncogenic virus. In this study, we engineered ribozymes derived from ribonuclease P (RNase P) catalytic RNA with targeting against the mRNA ... ...

    Abstract Kaposi's sarcoma, an AIDS-defining illness, is caused by Kaposi's sarcoma-associated herpesvirus (KSHV), an oncogenic virus. In this study, we engineered ribozymes derived from ribonuclease P (RNase P) catalytic RNA with targeting against the mRNA encoding KSHV immediate early replication and transcription activator (RTA), which is vital for KSHV gene expression. The functional ribozyme F-RTA efficiently sliced the RTA mRNA sequence in vitro. In cells, KSHV production was suppressed with ribozyme F-RTA expression by 250-fold, and RTA expression was suppressed by 92-94%. In contrast, expression of control ribozymes hardly affected RTA expression or viral production. Further studies revealed both overall KSHV early and late gene expression and viral growth decreased because of F-RTA-facilitated suppression of RTA expression. Our results indicate the first instance of RNase P ribozymes having potential for use in anti-KSHV therapy.
    MeSH term(s) Herpesvirus 8, Human/genetics ; Herpesvirus 8, Human/metabolism ; RNA, Catalytic/genetics ; RNA, Catalytic/metabolism ; Ribonuclease P/genetics ; Ribonuclease P/metabolism ; Immediate-Early Proteins/metabolism ; Virus Replication/genetics ; Virus Latency ; Trans-Activators/genetics ; RNA, Messenger/genetics ; Gene Expression ; Gene Expression Regulation, Viral
    Chemical Substances RNA, Catalytic ; Ribonuclease P (EC 3.1.26.5) ; Immediate-Early Proteins ; Trans-Activators ; RNA, Messenger
    Language English
    Publishing date 2023-04-21
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules28083619
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Development of Genome Editing Approaches against Herpes Simplex Virus Infections.

    Zhang, Isadora / Hsiao, Zoe / Liu, Fenyong

    Viruses

    2021  Volume 13, Issue 2

    Abstract: Herpes simplex virus 1 (HSV-1) is a herpesvirus that may cause cold sores or keratitis in healthy or immunocompetent individuals, but can lead to severe and potentially life-threatening complications in immune-immature individuals, such as neonates or ... ...

    Abstract Herpes simplex virus 1 (HSV-1) is a herpesvirus that may cause cold sores or keratitis in healthy or immunocompetent individuals, but can lead to severe and potentially life-threatening complications in immune-immature individuals, such as neonates or immune-compromised patients. Like all other herpesviruses, HSV-1 can engage in lytic infection as well as establish latent infection. Current anti-HSV-1 therapies effectively block viral replication and infection. However, they have little effect on viral latency and cannot completely eliminate viral infection. These issues, along with the emergence of drug-resistant viral strains, pose a need to develop new compounds and novel strategies for the treatment of HSV-1 infection. Genome editing methods represent a promising approach against viral infection by modifying or destroying the genetic material of human viruses. These editing methods include homing endonucleases (HE) and the Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)/CRISPR associated protein (Cas) RNA-guided nuclease system. Recent studies have showed that both HE and CRISPR/Cas systems are effective in inhibiting HSV-1 infection in cultured cells in vitro and in mice in vivo. This review, which focuses on recently published progress, suggests that genome editing approaches could be used for eliminating HSV-1 latent and lytic infection and for treating HSV-1 associated diseases.
    MeSH term(s) Animals ; Clustered Regularly Interspaced Short Palindromic Repeats ; Gene Editing/methods ; Genome, Viral ; Herpesviridae Infections/virology ; Herpesvirus 1, Human/genetics ; Herpesvirus 1, Human/physiology ; Humans
    Language English
    Publishing date 2021-02-22
    Publishing country Switzerland
    Document type Evaluation Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v13020338
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Book: Ribonuclease P

    Liu, Fenyong / Altman, Sidney

    (Protein reviews ; v. 10)

    2010  

    Author's details Fenyong Liu, Sidney Altman, editors
    Series title Protein reviews ; v. 10
    Keywords RNA. ; Ribonucleases.
    Language English
    Size xvi, 283 p. :, ill. (some col.) ;, 24 cm.
    Publisher Springer
    Publishing place New York
    Document type Book
    ISBN 9781441911414 ; 1441911413 ; 1441911421 ; 9781441911421
    Database NAL-Catalogue (AGRICOLA)

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  10. Book: Ribonuclease P

    Liu, Fenyong / Altman, Sidney

    (Protein reviews ; v. 10)

    2010  

    Author's details Fenyong Liu, Sidney Altman, editors
    Series title Protein reviews ; v. 10
    MeSH term(s) Ribonuclease P/metabolism ; Ribonuclease P/biosynthesis ; RNA
    Language English
    Size xvi, 283 p. :, ill. (some col.), port. ;, 24 cm.
    Publisher Springer
    Publishing place New York
    Document type Book
    ISBN 9781441911414 ; 1441911413 ; 9781441911421 ; 1441911421
    Database Catalogue of the US National Library of Medicine (NLM)

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