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2′-deoxy-2′-fluoro pyrimidine nucleotides 2′-fluoro-modified ctp and utp  (TriLink)

 
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    TriLink 2′-deoxy-2′-fluoro pyrimidine nucleotides 2′-fluoro-modified ctp and utp
    2′ Deoxy 2′ Fluoro Pyrimidine Nucleotides 2′ Fluoro Modified Ctp And Utp, supplied by TriLink, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/2%E2%80%B2-deoxy-utp/2++fluoro+utp/pmc04990464-176-42-53
    Average 90 stars, based on 1 article reviews
    2′-deoxy-2′-fluoro pyrimidine nucleotides 2′-fluoro-modified ctp and utp - by Bioz Stars, 2026-08
    90/100 stars

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    Figure 3. An intact 3′ - hydroxyl group on the ribose of a 3′-terminal UMP is essential for H1085Y-mediated intrinsic cleavage. ( A ) As outlined, RNAP II EC32 (elongation complex with 32-mer RNA) complexes were divided and their nascent RNAs were extended by 1 nt with either UTP, <t>3′-deoxy-UTP</t> or 2′-deoxy-UTP. Washes omitting metal cofactors are delineated as “-Me 2+ .” Following a washing step in the absence of metal cofactors, ECs were then exposed to Mn 2+ ions to initiate intrinsic cleavage where appropriate. ( B ) Comparison of cleavage reactions by WT (RNA lengths; 32, 33 nt) and H1085Y (RNA lengths; 32, 33 nt) RNAP II enzymes. A terminal 3′-dUMP prevented RNA hydrolysis by H1085Y RNAP II ( lane 12 ), while the WT RNAP II control lanes reveal little WT RNAP II cleavage activity regardless of the nature of the 3′-NMP added. ( C ) Structures of the tested 3′-NMP modified sugars are depicted. Experiments are representative of at least two independent determinations.
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    Figure 3. An intact 3′ - hydroxyl group on the ribose of a 3′-terminal UMP is essential for H1085Y-mediated intrinsic cleavage. ( A ) As outlined, RNAP II EC32 (elongation complex with 32-mer RNA) complexes were divided and their nascent RNAs were extended by 1 nt with either UTP, 3′-deoxy-UTP or 2′-deoxy-UTP. Washes omitting metal cofactors are delineated as “-Me 2+ .” Following a washing step in the absence of metal cofactors, ECs were then exposed to Mn 2+ ions to initiate intrinsic cleavage where appropriate. ( B ) Comparison of cleavage reactions by WT (RNA lengths; 32, 33 nt) and H1085Y (RNA lengths; 32, 33 nt) RNAP II enzymes. A terminal 3′-dUMP prevented RNA hydrolysis by H1085Y RNAP II ( lane 12 ), while the WT RNAP II control lanes reveal little WT RNAP II cleavage activity regardless of the nature of the 3′-NMP added. ( C ) Structures of the tested 3′-NMP modified sugars are depicted. Experiments are representative of at least two independent determinations.

    Journal: Transcription

    Article Title: Activation and reactivation of the RNA polymerase II trigger loop for intrinsic RNA cleavage and catalysis

    doi: 10.4161/trns.28869

    Figure Lengend Snippet: Figure 3. An intact 3′ - hydroxyl group on the ribose of a 3′-terminal UMP is essential for H1085Y-mediated intrinsic cleavage. ( A ) As outlined, RNAP II EC32 (elongation complex with 32-mer RNA) complexes were divided and their nascent RNAs were extended by 1 nt with either UTP, 3′-deoxy-UTP or 2′-deoxy-UTP. Washes omitting metal cofactors are delineated as “-Me 2+ .” Following a washing step in the absence of metal cofactors, ECs were then exposed to Mn 2+ ions to initiate intrinsic cleavage where appropriate. ( B ) Comparison of cleavage reactions by WT (RNA lengths; 32, 33 nt) and H1085Y (RNA lengths; 32, 33 nt) RNAP II enzymes. A terminal 3′-dUMP prevented RNA hydrolysis by H1085Y RNAP II ( lane 12 ), while the WT RNAP II control lanes reveal little WT RNAP II cleavage activity regardless of the nature of the 3′-NMP added. ( C ) Structures of the tested 3′-NMP modified sugars are depicted. Experiments are representative of at least two independent determinations.

    Article Snippet: rNTPs and 2′-deoxy-dATP were obtained from GE Healthcare Life Sciences; [α- 32 P] ATP and [γ- 32 P ] ATP from Perkin-Elmer; 2′-deoxy-UTP, 3′-deoxy-UTP and dinucleotide GpG from TriLink Biotechnologies.

    Techniques: Comparison, Control, Activity Assay, Modification