New sequence-specific human ribonuclease: purification and properties.

G Przewlocki; J Lipecka; A Edelman; A Przykorska

doi:10.1093/nar/26.17.4047

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PubMed · 9705518

New sequence-specific human ribonuclease: purification and properties.

G Przewlocki·J Lipecka·A Edelman·A Przykorska

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Abstract

A new sequence-specific RNase was isolated from human colon carcinoma T84 cells. The enzyme was purified to electrophoretical homogeneity by pH precipitation, HiTrapSP and Superdex 200 FPLC. The molecular weight of the new enzyme, which we have named RNase T84, is 19 kDa. RNase T84 is an endonuclease which generates 5'-phosphate-terminated products. The new RNase selectively cleaved the phosphodiester bonds at AU or GU steps at the 3' side of A or G and the 5' side of U. 5'AU3' or 5'GU3' is the minimal sequence required for T84 RNase activity, but the rate of cleavage depends on the sequence and/or structure context. Synthetic ribohomopolymers such as poly(A), poly(G), poly(U) and poly(C) were very poorly hydrolysed by T84 enzyme. In contrast, poly(I) and heteroribopolymers poly(A,U) and poly(A,G,U) were good substrates for the new RNase. The activity towards poly(I) was stronger in two colon carcinoma cell lines than in three other epithelial cell lines. Our results show that RNase T84 is a new sequence-specific enzyme whose gene is abundantly expressed in human colon carcinoma cell lines.

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Adenocarcinoma Base Sequence Biomarkers, Tumor Colonic Neoplasms Endoribonucleases Humans Molecular Sequence Data Neoplasm Proteins Nucleic Acid Conformation Poly A-U Poly I Polyribonucleotides RNA, Transfer, Asp RNA, Transfer, Phe Substrate Specificity Tumor Cells, Cultured Comparative Study Journal Article Research Support, Non-U.S. Gov't

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G Przewlocki, J Lipecka, A Edelman, A Przykorska. 1998-09-01. New sequence-specific human ribonuclease: purification and properties.. https://doi.org/10.1093/nar%2F26.17.4047

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