Scholarlink

<p>Bacteriophages use diverse genomic modifications, including substitutions on the cytosine pyrimidine ring through C–C and C–N bonds. Here, we report that coliphage HY126 encodes an Afh system with enzymatic activities not previously implicated in DNA modification. This multienzyme cascade comprises the following: AfhB, a reduced flavin-dependent hydroxylase that catalyzes deoxycytidine monophosphate (dCMP) hydroxylation through C–O bond formation to yield 5-hydroxy-dCMP; AfhE and AfhF, which synthesize the sugar donor uridine diphospho-<span>ᴅ</span>-arabinose for AfhC; AfhC, a phage-encoded nucleotide arabinosyltransferase that arabinofuranosylates 5-hydroxy-dCMP, priming it for DNA incorporation; AfhG, a DNA arabinosyltransferase that adds a second arabinofuranose moiety through a β-1,3 linkage to 5-hydroxyarabinofuranosylated cytosine embedded in DNA, forming diarabinofuranosyl-5-hydroxycytosine. This work unveils a unique two-step arabinofuranosylation mechanism—involving distinct nucleotide priming followed by DNA modification—thereby elucidating an enzymatic strategy in the phage–host evolutionary arms race.</p><p></p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Dual cytosine modification through hydroxylation and arabinofuranosylation in phages

  • 期刊论文

  • 发表日期：

    2026年4月1日

查看全文
  • Yu He,
  • Haiyan Gao,
  • Yudong Yang,
  • Dongang Yang,
  • Lixu Jiang,
  • Junwu Bi,
  • Fuliang Yin,
  • Yaru Tang,
  • Zhe Zhao,
  • Shi Chen,
  • Lianrong Wang

摘要

Bacteriophages use diverse genomic modifications, including substitutions on the cytosine pyrimidine ring through C–C and C–N bonds. Here, we report that coliphage HY126 encodes an Afh system with enzymatic activities not previously implicated in DNA modification. This multienzyme cascade comprises the following: AfhB, a reduced flavin-dependent hydroxylase that catalyzes deoxycytidine monophosphate (dCMP) hydroxylation through C–O bond formation to yield 5-hydroxy-dCMP; AfhE and AfhF, which synthesize the sugar donor uridine diphospho-ᴅ-arabinose for AfhC; AfhC, a phage-encoded nucleotide arabinosyltransferase that arabinofuranosylates 5-hydroxy-dCMP, priming it for DNA incorporation; AfhG, a DNA arabinosyltransferase that adds a second arabinofuranose moiety through a β-1,3 linkage to 5-hydroxyarabinofuranosylated cytosine embedded in DNA, forming diarabinofuranosyl-5-hydroxycytosine. This work unveils a unique two-step arabinofuranosylation mechanism—involving distinct nucleotide priming followed by DNA modification—thereby elucidating an enzymatic strategy in the phage–host evolutionary arms race.