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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : Current opinion in structural biology

Terminal deoxynucleotidyltransferase: the story of an untemplated DNA polymerase capable of DNA bridging and templated synthesis across strands

Team: Architecture and Dynamics of Biological Macromolecules
Member: Marc Delarue
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Current opinion in structural biology - 12 Apr 2018

Loc'h J, Delarue M

Link to Pubmed [PMID] – 29656238

Link to HAL – Click here

Link to DOI – 10.1016/j.sbi.2018.03.019

Curr. Opin. Struct. Biol. 2018 12;53:22-31

Terminal deoxynucleotidyltransferase (TdT) is a member of the polX family which is involved in DNA repair. It has been known for years as an untemplated DNA polymerase used during V(D)J recombination to generate diversity at the CDR3 region of immunoglobulins and T-cell receptors. Recently, however, TdT was crystallized in the presence of a complete DNA synapsis made of two double-stranded DNA (dsDNA), each with a 3′ protruding end, and overlapping with only one micro-homology base-pair, thus giving structural insight for the first time into DNA synthesis across strands. It was subsequently shown that TdT indeed has an in trans template-dependent activity in the presence of an excess of the downstream DNA duplex. A possible biological role of this dual activity is discussed.