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    SRP72 signal recognition particle 72 [ Homo sapiens (human) ]

    Gene ID: 6731, updated on 4-Jan-2025

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    e show that SRP RNA does not bind to the ribosome, while SRP binds with nanomolar affinity involving a two-step mechanism of the key-player SRP54. Ultrasensitive binding of SRP68/72 indicates avidity by multiple binding sites that are dominated by the C-terminus of SRP72

    Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions.
    Wild K, Juaire KD, Soni K, Shanmuganathan V, Hendricks A, Segnitz B, Beckmann R, Sinning I., Free PMC Article

    10/12/2019
    SRP72 depletion is associated with elevated levels of apoptosis after irradiation.

    Depletion of signal recognition particle 72kDa increases radiosensitivity.
    Prevo R, Tiwana GS, Maughan TS, Buffa FM, McKenna WG, Higgins GS., Free PMC Article

    04/28/2018
    The essential role of the SRP68-SRP72 interaction in the signal recognition particle-mediated protein translocation

    Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation.
    Gao Y, Zhang Q, Lang Y, Liu Y, Dong X, Chen Z, Tian W, Tang J, Wu W, Tong Y, Chen Z., Free PMC Article

    04/7/2018
    The crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP have been presented.

    Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.
    Becker MM, Lapouge K, Segnitz B, Wild K, Sinning I., Free PMC Article

    06/10/2017
    SRP68/72 heterodimers as major nuclear proteins whose binding of histone H4 tail is inhibited by H4R3 methylation.

    A novel histone H4 arginine 3 methylation-sensitive histone H4 binding activity and transcriptional regulatory function for signal recognition particle subunits SRP68 and SRP72.
    Li J, Zhou F, Zhan D, Gao Q, Cui N, Li J, Iakhiaeva E, Zwieb C, Lin B, Wong J., Free PMC Article

    03/2/2013
    A heterozygous mutation in SRP72 has a role in familial aplasia and myelodysplasia.

    Exome sequencing identifies autosomal-dominant SRP72 mutations associated with familial aplasia and myelodysplasia.
    Kirwan M, Walne AJ, Plagnol V, Velangi M, Ho A, Hossain U, Vulliamy T, Dokal I., Free PMC Article

    06/30/2012
    The study delineated the minimal region of SRP72 capable of forming a stable complex with an signal recognition particle RNA fragment.

    Identification of amino acid residues in protein SRP72 required for binding to a kinked 5e motif of the human signal recognition particle RNA.
    Iakhiaeva E, Iakhiaev A, Zwieb C., Free PMC Article

    02/26/2011
    Inhibitors of MAPK pathway ERK1/2 or p38 prevent the IL-1{beta}-induced up-regulation of SRP72 autoantigen in Jurkat cells.

    Inhibitors of MAPK pathway ERK1/2 or p38 prevent the IL-1{beta}-induced up-regulation of SRP72 autoantigen in Jurkat cells.
    Arana-Argáez VE, Delgado-Rizo V, Pizano-Martínez OE, Martínez-Garcia EA, Martín-Márquez BT, Muñoz-Gómez A, Petri MH, Armendáriz-Borunda J, Espinosa-Ramírez G, Zúñiga-Tamayo DA, Herrera-Esparza R, Vázquez-Del Mercado M., Free PMC Article

    11/27/2010
    Human signal recognition particle RNA with a single A240G change was unable to form a complex with full-length human SRP72.

    The 5e motif of eukaryotic signal recognition particle RNA contains a conserved adenosine for the binding of SRP72.
    Iakhiaeva E, Wower J, Wower IK, Zwieb C., Free PMC Article

    01/21/2010
    Human SRP RNA bound with high affinity to a 63 amino acid residue region near the C terminus of SRP72

    Identification of an RNA-binding domain in human SRP72.
    Iakhiaeva E, Yin J, Zwieb C.

    01/21/2010
    Ninety-four amino acids near the C terminus of SRP68 mediated the binding to SRP72

    Protein SRP68 of human signal recognition particle: identification of the RNA and SRP72 binding domains.
    Iakhiaeva E, Bhuiyan SH, Yin J, Zwieb C., Free PMC Article

    01/21/2010
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