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diff --git a/biblio/29741723.mdwn b/biblio/29741723.mdwn
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+[[!meta title="A single-molecule sequencing assay for the comprehensive profiling of T4 DNA ligase fidelity and bias during DNA end-joining."]]
+[[!tag enzyme ligase]]
+
+Nucleic Acids Res. 2018 Jul 27;46(13):e79. doi:10.1093/nar/gky303
+
+Potapov V, Ong JL, Langhorst BW, Bilotti K, Cahoon D, Canton B, Knight TF,
+Evans TC Jr, Lohman GJS.
+
+A single-molecule sequencing assay for the comprehensive profiling of T4 DNA ligase fidelity and bias during DNA end-joining.
+
+[[!pmid 29741723 desc="TNA overhangs are very inefficient to ligate.  However ANT are not harder to ligate than similar mismatches.  GC-rich overhangs better tolerate mismatches than AT-rich ones.  Increasing temperature reduced mismatched ligations.  5′-G mismatches are much better tolerated than 5′-T mismatches."]]

diff --git a/tags/ligase.mdwn b/tags/ligase.mdwn
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--- a/tags/ligase.mdwn
+++ b/tags/ligase.mdwn
@@ -51,6 +51,15 @@ DNA and RNA ligases can be used to adenylylate a substrate.
  - [[Torchia, Takagi and Ho (2008)|biblio/18829718]] reported the use
    of the Methanobacterium RNA ligase (MthRnl) to adenylylate RNA.
 
+## Sequence biases
+
+(work in progress)
+
+ - Potapov and coll. ([[2018|biblio/29741723]]) studied in details the tolerance
+   to mismatches of T4 DNA ligase when ligating 3' overhangs.  Mismatches were
+   better tolerated with higher GC content and lower temperature.  Surprisingly,
+   TNA overhangs were especially hard to ligate.
+
 [[!inline pages="tagged(ligase)" limit=0]]
 [[!meta title="pages tagged adenylylation"]]