DDE transposases: Structural similarity and diversity

Irina V. Nesmelova, Perry B Hackett

Research output: Contribution to journalReview article

38 Citations (Scopus)

Abstract

DNA transposons are mobile DNA elements that can move from one DNA molecule to another and thereby deliver genetic information into human chromosomes in order to confer a new function or replace a defective gene. This process requires a transposase enzyme. During transposition DD[E/D]-transposases undergo a series of conformational changes. We summarize the structural features of DD[E/D]-transposases for which three-dimensional structures are available and that relate to transposases, which are being developed for use in mammalian cells. Similar to other members of the polynucleotidyl transferase family, the catalytic domains of DD[E/D]-transposases share a common feature: an RNase H-like fold that draws three catalytically active residues, the DDE motif, into close proximity. Beyond this fold, the structures of catalytic domains vary considerably, and the DD[E/D]-transposases display marked structural diversity within their DNA-binding domains. Yet despite such structural variability, essentially the same end result is achieved.

Original languageEnglish (US)
Pages (from-to)1187-1195
Number of pages9
JournalAdvanced Drug Delivery Reviews
Volume62
Issue number12
DOIs
StatePublished - Sep 30 2010

Fingerprint

Transposases
Dichlorodiphenyl Dichloroethylene
DNA
Catalytic Domain
Ribonuclease H
DNA Transposable Elements
Human Chromosomes
Transferases
Enzymes
Genes

Keywords

  • DD[E/D]-transposase
  • DNA transposon
  • Structure
  • Transposase

Cite this

DDE transposases : Structural similarity and diversity. / Nesmelova, Irina V.; Hackett, Perry B.

In: Advanced Drug Delivery Reviews, Vol. 62, No. 12, 30.09.2010, p. 1187-1195.

Research output: Contribution to journalReview article

Nesmelova, Irina V. ; Hackett, Perry B. / DDE transposases : Structural similarity and diversity. In: Advanced Drug Delivery Reviews. 2010 ; Vol. 62, No. 12. pp. 1187-1195.
@article{2b2e4a9601d24a6d8ebac2f0eb644417,
title = "DDE transposases: Structural similarity and diversity",
abstract = "DNA transposons are mobile DNA elements that can move from one DNA molecule to another and thereby deliver genetic information into human chromosomes in order to confer a new function or replace a defective gene. This process requires a transposase enzyme. During transposition DD[E/D]-transposases undergo a series of conformational changes. We summarize the structural features of DD[E/D]-transposases for which three-dimensional structures are available and that relate to transposases, which are being developed for use in mammalian cells. Similar to other members of the polynucleotidyl transferase family, the catalytic domains of DD[E/D]-transposases share a common feature: an RNase H-like fold that draws three catalytically active residues, the DDE motif, into close proximity. Beyond this fold, the structures of catalytic domains vary considerably, and the DD[E/D]-transposases display marked structural diversity within their DNA-binding domains. Yet despite such structural variability, essentially the same end result is achieved.",
keywords = "DD[E/D]-transposase, DNA transposon, Structure, Transposase",
author = "Nesmelova, {Irina V.} and Hackett, {Perry B}",
year = "2010",
month = "9",
day = "30",
doi = "10.1016/j.addr.2010.06.006",
language = "English (US)",
volume = "62",
pages = "1187--1195",
journal = "Advanced Drug Delivery Reviews",
issn = "0169-409X",
publisher = "Elsevier",
number = "12",

}

TY - JOUR

T1 - DDE transposases

T2 - Structural similarity and diversity

AU - Nesmelova, Irina V.

AU - Hackett, Perry B

PY - 2010/9/30

Y1 - 2010/9/30

N2 - DNA transposons are mobile DNA elements that can move from one DNA molecule to another and thereby deliver genetic information into human chromosomes in order to confer a new function or replace a defective gene. This process requires a transposase enzyme. During transposition DD[E/D]-transposases undergo a series of conformational changes. We summarize the structural features of DD[E/D]-transposases for which three-dimensional structures are available and that relate to transposases, which are being developed for use in mammalian cells. Similar to other members of the polynucleotidyl transferase family, the catalytic domains of DD[E/D]-transposases share a common feature: an RNase H-like fold that draws three catalytically active residues, the DDE motif, into close proximity. Beyond this fold, the structures of catalytic domains vary considerably, and the DD[E/D]-transposases display marked structural diversity within their DNA-binding domains. Yet despite such structural variability, essentially the same end result is achieved.

AB - DNA transposons are mobile DNA elements that can move from one DNA molecule to another and thereby deliver genetic information into human chromosomes in order to confer a new function or replace a defective gene. This process requires a transposase enzyme. During transposition DD[E/D]-transposases undergo a series of conformational changes. We summarize the structural features of DD[E/D]-transposases for which three-dimensional structures are available and that relate to transposases, which are being developed for use in mammalian cells. Similar to other members of the polynucleotidyl transferase family, the catalytic domains of DD[E/D]-transposases share a common feature: an RNase H-like fold that draws three catalytically active residues, the DDE motif, into close proximity. Beyond this fold, the structures of catalytic domains vary considerably, and the DD[E/D]-transposases display marked structural diversity within their DNA-binding domains. Yet despite such structural variability, essentially the same end result is achieved.

KW - DD[E/D]-transposase

KW - DNA transposon

KW - Structure

KW - Transposase

UR - http://www.scopus.com/inward/record.url?scp=78649326287&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78649326287&partnerID=8YFLogxK

U2 - 10.1016/j.addr.2010.06.006

DO - 10.1016/j.addr.2010.06.006

M3 - Review article

C2 - 20615441

AN - SCOPUS:78649326287

VL - 62

SP - 1187

EP - 1195

JO - Advanced Drug Delivery Reviews

JF - Advanced Drug Delivery Reviews

SN - 0169-409X

IS - 12

ER -