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Summary[edit | edit source]

  • pan ID?: SAUPAN003376000
  • symbol?: rnhC
  • synonym:
  • description?: ribonuclease HIII

      descriptions from strain specific annotations:

    • ribonuclease HIII
    • putative ribonuclease
  • strand?: -
  • coordinates?: 3739984..3740925
  • synteny block?: BlockID0024590
  • occurrence?: in 100% of 34 strains

rnhC : ribonuclease H-III [1]

Staphylococci produce different paralogues of Ribonuclease H to introduce nicks in different RNA-DNA hybrid structures. The most prevalent RNA-DNA hybrids in bacteria are Okazaki fragments generated during lagging strand synthesis. RNase H-III introduces a nick 5'- to a string of ribonucleotides in a DNA-RNA duplex. The nick allows DNA Pol I access to the ribonucleotides which it removes with its 5'→3' exonuclease activity and then fills in with deoxyribonucleotides. Alternatively, the exonuclease function can be accomplished using the 5'→3' flap riboexonuclease Fen, although DNA polymerase is still required to fill in the new ssDNA region. In bacteria such as E. coli, the RNase H-III activity is performed by RNase H-I. However, in Bacillus subtilis, RNase H-I is catalytically inactive and functionally-replaced with RNase H-III. Staphylococci do encode an RNase H-I orthologue but its catalytic activity is not clear.

Orthologs[edit | edit source]

    COL:
    SACOL1150 (rnhC)
    N315:
    NCTC8325:
    Newman:
    USA300_FPR3757:
    04-02981:
    SA2981_1096
    08BA02176:
    C248_1167
    11819-97:
    MS7_1096 (rnhC)
    6850:
    RSAU_001024 (rnhC)
    71193:
    ST398NM01_1136
    ECT-R 2:
    ECTR2_994 (rnhC)
    ED133:
    SAOV_1136c
    ED98:
    SAAV_1107 (rnhC)
    HO 5096 0412:
    SAEMRSA15_09700
    JH1:
    SaurJH1_1221
    JH9:
    SaurJH9_1199
    JKD6008:
    SAA6008_01094 (rnhC)
    JKD6159:
    SAA6159_00994 (rnhC)
    JSNZ:
    JSNZ_001105 (rnhC)
    LGA251:
    SARLGA251_10520
    M013:
    M013TW_1073
    MRSA252:
    SAR1113
    MSHR1132:
    SAMSHR1132_09860
    MSSA476:
    SAS1074
    Mu3:
    SAHV_1131
    Mu50:
    SAV1140
    MW2:
    MW1023
    RF122:
    SAB1004c
    ST398:
    SAPIG1136 (rnhC)
    T0131:
    SAT0131_01182
    TCH60:
    HMPREF0772_12093 (rnhC)
    TW20:
    SATW20_11340 (rnhC)
    USA300_TCH1516:
    USA300HOU_1075 (rnhC)
    VC40:
    SAVC_04865

Genome Viewer[edit | edit source]

COL
N315
NCTC8325
Newman
USA300_FPR3757

Alignments[edit | edit source]

  • alignment of orthologues:
    CLUSTAL format alignment by MAFFT L-INS-i (v7.307)


    COL             MANIVFKLSDKDITTLMSRISFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
    N315            MANIVFKLSDKDITTLMSRITFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
    NCTC8325        MANIVFKLSDKDITTLMSRISFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
    Newman          MANIVFKLSDKDITTLMSRISFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
    USA300_FPR3757  MANIVFKLSDKDITTLMSRISFDTENLPQGMKARAKYQNTTVNIYQSGKVMFQGNHAEAV
                    ********************:***************************************

    COL             SEELLPQHSQLNTNKTKKKNMANSFLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
    N315            SKELLPQHSQLNTNKTKKKNMANSSLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
    NCTC8325        SEELLPQHSQLNTNKTKKKNMANSFLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
    Newman          SEELLPQHSQLNTNKTKKKNMANSFLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
    USA300_FPR3757  SEELLPQHSQLNTNKTKKKNMANSFLEQTLMYDQFNCIGSDEAGSGDYFGPLTVCAAFVT
                    *:********************** ***********************************

    COL             KEHVPILKTLGVDDSKKLTDTKIVELAEQLVTFIPHSLLTLHNEKYNIQQAKGWTQVKMK
    N315            KEHVPILKTLGVDDSKKLTDTKIVELAEQLVAFIPHSLLTLHNDKYNIQQAKGWTQVKMK
    NCTC8325        KEHVPILKTLGVDDSKKLTDTKIVELAEQLVTFIPHSLLTLHNEKYNIQQAKGWTQVKMK
    Newman          KEHVPILKTLGVDDSKKLTDTKIVELAEQLVTFIPHSLLTLHNEKYNIQQAKGWTQVKMK
    USA300_FPR3757  KEHVPILKTLGVDDSKKLTDTKIVELAEQLVTFIPHSLLTLHNEKYNIQQAKGWTQVKMK
                    *******************************:***********:****************

    COL             AALHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
    N315            AVLHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
    NCTC8325        AALHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
    Newman          AALHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
    USA300_FPR3757  AALHNEAIKNVLEKIDSSQLDYIVIDQFAKREVYSHYALSDIPLPKKTKFETKGESKSLA
                    *.**********************************************************

    COL             IAVASIISRYAFVTYMDQISKNINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
    N315            IAVASIISRYAFITYMDQISKYINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
    NCTC8325        IAVASIISRYAFVTYMDQISKNINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
    Newman          IAVASIISRYAFVTYMDQISKNINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
    USA300_FPR3757  IAVASIISRYAFVTYMDQISKNINMTIPKGAGAKVDVIAAKIIKKYGLSRLDTISKKHFK
                    ************:******** **************************************

    COL             NREKAQKILKPL
    N315            NREKAQKILKPL
    NCTC8325        NREKAQKILKPL
    Newman          NREKAQKILKPL
    USA300_FPR3757  NREKAQKILKPL
                    ************

  1. Scott A Reiling, Kohei Homma, Oluwatoyin A Asojo
    Purification and crystallization of RNase HIII from Staphylococcus aureus.
    Acta Crystallogr Sect F Struct Biol Cryst Commun: 2011, 67(Pt 1);79-82
    [PubMed:21206030] [WorldCat.org] [DOI] (I p)
    Justin R Randall, William G Hirst, Lyle A Simmons
    Substrate Specificity for Bacterial RNases HII and HIII Is Influenced by Metal Availability.
    J Bacteriol: 2018, 200(4);
    [PubMed:29084857] [WorldCat.org] [DOI] (I e)
    Justin R Randall, Taylor M Nye, Katherine J Wozniak, Lyle A Simmons
    RNase HIII Is Important for Okazaki Fragment Processing in Bacillus subtilis.
    J Bacteriol: 2019, 201(7);
    [PubMed:30670546] [WorldCat.org] [DOI] (I e)
    Anna Lipońska, Mee-Ngan F Yap
    Hibernation-Promoting Factor Sequesters Staphylococcus aureus Ribosomes to Antagonize RNase R-Mediated Nucleolytic Degradation.
    mBio: 2021, 12(4);e0033421
    [PubMed:34253058] [WorldCat.org] [DOI] (I p)