The specific endoribonuclease activity of small nuclear and cytoplasmic α‐RNPs

FEBS Letters

Gause, L.N.²  Mittenberg, A.G.¹  Volkova, I.V.¹  Kulichkova, V.A.¹  Ermolaeva, J.B.¹  Evteeva, I.N.¹  Konstantinova, I.M.¹ 

[1] Institute of Cytology, Russian Academy of Sciences, Tikhoretsky av. 4, St.-Petersburg 194064, Russia;Kol'tsov Institute of Developmental Biology, Russian Academy of Sciences, Moscow Russia

关键词: Small α-ribonucleoprotein particle;    Endoribonuclease activity;    RNase;    mRNA stability;    Short interspersed repeat;    Prosome;    Proteasome;    mRNA;    messenger RNA;    PAGE;    polyacrylamide gel electrophoresis;    DMSO;    dimethylsulfoxide;    hmwRNA;    high-molecular-weight RNA;    lmwRNA;    low-molecular-weight RNA;    RNP;    ribonucleoprotein particle;    n-αRNP;    nuclear α-RNP;    c-αRNP;    cytoplasmic α-RNP;    hnRNA;    heterogeneous nuclear RNA;   

DOI  :  10.1016/S0014-5793(99)01565-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

For the first time small nuclear ribonucleoprotein particles (α-RNP) tightly bound to chromatin as well as cytoplasmic α-RNP are shown to possess strong and regulated endonuclease activity specific for mRNAs and hnRNAs. The enzymatic nature of this activity is confirmed, and the optimal conditions detected. This RNase activity is controlled by the action of a differentiating stimulus, dimethylsulfoxide, in human K562 cells. Small α-RNP involvement in the coordinated control of stability of pre-messenger RNA and messenger RNA molecules is suggested.

【 授权许可】

Unknown