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Cited by 401

The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.

Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins

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Aravind, L·1998·Nucleic Acids Research
DOI 10.1093/nar/26.18.4205
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Abstract

Iterative profile searches and structural modeling show that bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, type IA and type II topoisomerases, bacterial and archaeal nucleases of the OLD family and bacterial DNA repair proteins of the RecR/M family contain a common domain, designated Toprim (topoisomerase-primase) domain. The domain consists of approximately 100 amino acids and has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). Examination of the structure of Topo IA and Topo II and modeling of the Toprim domains of the primases reveal a compact beta/alpha fold, with the conserved negatively charged residues juxtaposed, and inserts seen in Topo IA and Topo II. The conserved glutamate may act as a general base in nucleotide polymerization by primases and in strand rejoining by topoisomerases and as a general acid in strand cleavage by topoisomerases and nucleases. The role of this glutamate in catalysis is supported by site-directed mutagenesis data on primases and Topo IA. The DxD motif may coordinate Mg2+that is required for the activity of all Toprim-containing enzymes. The common ancestor of all life forms could encode a prototype Toprim enzyme that might have had both nucleotidyl transferase and polynucleotide cleaving activity.

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Metadata

Authors
Aravind, L.
Venue
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Published
1998-09-15
Volume
26
Issue
18
Pages
4205-4213
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
DOI
10.1093/nar/26.18.4205
OpenAlex
W2098891503
Cited by
401
References
58
FWCI
4.05
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. https://app.cochat.ai/papers/10.1093/nar/26.18.4205
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Aravind, L. (1998). Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Nucleic Acids Research. https://doi.org/10.1093/nar/26.18.4205

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