6ZOP

Structure of the cysteine-rich domain of PiggyMac, a domesticated PiggyBac transposase involved in programmed genome rearrangements

Summary for 6ZOP

• Entry DOI: 10.2210/pdb6zop/pdb
• NMR Information: BMRB: 34527
• Descriptor: DDE_Tnp_1_7 domain-containing protein, ZINC ION (2 entities in total)
• Functional Keywords: zinc-finger, transposase, piggymac, cysteine-riche domain, gene regulation
• Biological source: Paramecium tetraurelia
• Total number of polymer chains: 1
• Total formula weight: 9803.90

Authors

Bessa, L.,Guerineau, M.,Moriau, S.,Lescop, E.,Bontems, F.,Mathy, N.,Guittet, E.,Bischerour, J.,Betermier, M.,Morellet, N. (deposition date: 2020-07-07, release date: 2021-06-16, Last modification date: 2024-01-31)

Primary citation

Guerineau, M.,Bessa, L.,Moriau, S.,Lescop, E.,Bontems, F.,Mathy, N.,Guittet, E.,Bischerour, J.,Betermier, M.,Morellet, N.
The unusual structure of the PiggyMac cysteine-rich domain reveals zinc finger diversity in PiggyBac-related transposases.
Mob DNA, 12:12-12, 2021

PubMed Abstract: Transposons are mobile genetic elements that colonize genomes and drive their plasticity in all organisms. DNA transposon-encoded transposases bind to the ends of their cognate transposons and catalyze their movement. In some cases, exaptation of transposon genes has allowed novel cellular functions to emerge. The PiggyMac (Pgm) endonuclease of the ciliate Paramecium tetraurelia is a domesticated transposase from the PiggyBac family. It carries a core catalytic domain typical of PiggyBac-related transposases and a short cysteine-rich domain (CRD), flanked by N- and C-terminal extensions. During sexual processes Pgm catalyzes programmed genome rearrangements (PGR) that eliminate ~ 30% of germline DNA from the somatic genome at each generation. How Pgm recognizes its DNA cleavage sites in chromatin is unclear and the structure-function relationships of its different domains have remained elusive.

PubMed: 33926516
DOI: 10.1186/s13100-021-00240-4

Experimental method

SOLUTION NMR