Distinct and opposite diversifying activities of terminal transferase splice variants.

Abstract:

The short splice variant of mouse terminal deoxynucleotidyl ...
The short splice variant of mouse terminal deoxynucleotidyl transferase (TdTS) catalyzes the addition of nontemplated nucleotides (N addition) at the coding joins of B cell and T cell antigen receptor genes. However, the activity and function of the long isoform of TdT (TdTL) have not been determined. We show here, in vitro and in vivo, that TdTL is a 3'-->5' exonuclease that catalyzes the deletion of nucleotides at coding joins. These findings suggest that the two TdT isoforms may act in concert to preserve the integrity of the variable region of antigen receptors while generating diversity.

Polymerases:

Topics:

Exonuclease Activity, Terminal Transferase

Status:

new topics/pols set partial results complete validated

Results:

Polymerase Reference Property Result Context
Terminal Transferase Distinct and opposite diversifying activities of terminal transferase splice variants. Terminal Transferase Yes
Terminal Transferase Distinct and opposite diversifying activities of terminal transferase splice variants. 5-3' Exonuclease Yes

Entry validated by:

Using Polbase tables:

Sorting:

Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).

Filtering:

It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.