Exonucleases (ExN) cleave nucleotides at the end of a polynucleotide chain[1]. In E. coli there are ExN I to VIII. ExN were found in human and yeast as well.


  • ExN-I cleaves single-stranded DNA.
  • ExN-II is associated with DNA polymerase.
  • ExN-III cleaves double-stranded DNA.
  • ExN-IV cleavage results in nucleoside monophosphate.
  • ExN-V cleaves linear double-stranded DNA.
  • ExN-VIII requires a free 5’ OH group for reacting.
  • For phage ExN see Sand box 211.

in E. coli exonuclease I (PDB code 1fxx).[2] Water molecules shown as red spheres.

E. coli exonuclease I complex with phosphate, glycerol and Mg+2 ion (PDB code 1fxx)

Drag the structure with the mouse to rotate

3D Structures of exonuclease3D Structures of exonuclease

Updated on 14-March-2019 {{#tree:id=OrganizedByTopic|openlevels=0|

  • ExN-I
  • ExN-III
  • ExN-IV
    • 2jc4 – ExN-IV – Nisseria meningitides
  • ExN-V
    • 1w36, 3k70 – EcExN-V α+β+γ + DNA hairpin
    • 3e1s - EcExN-V RECD subunit
    • 3gp8 - DrExN-V RECD subunit + DNA – Deinococcus radiodurans
    • 3gpl - DrExN-V RECD subunit + DNA + ADPNP
  • ExN-VII
    • 1vp7 – ExN-VII small subunit – Bordetella pertussis
  • ExN-VIII
    • 3h4r - EcExN-VIII C terminal (mutant)
  • ExN-X
  • 5’ ExN or exodeoxyribonuclease
    • 1ut5, 1ut8 – T5-5’-ExN + metal – Bacteriophage T5
    • 1exn, 1xo1 - T5-5’-ExN (mutant)
    • 5hmm - EpT5-5’-ExN + metal – Escherichia phage T5
    • 5hml - EpT5-5’-ExN (mutant) + metal
    • 5hnk, 5hp4 - EpT5-5’-ExN (mutant) + metal + DNA
    • 1avq – BlExN λ (mutant) – Bacteriophage λ
    • 3slp, 4wuz - BlExN λ + DNA
    • 3sm4 - BlExN λ (mutant) + DNA
    • 3k93 – ExN – Haemophilus somnus
  • ssDNA-specific ExN
    • 5ght – TkExN – Thermococcus kodakarensis
    • 5ghs, 5ghr – TkExN + polypeptide
    • 5f54 – DrExN + dTMP
    • 5f55 – DrExN + DNA
    • 5f56 – DrExN + DNA + polypeptide
  • 3'-5' ExN
    • 4yor, 4yot, 4you – PhExN phoexo I – Pyrococcus horikoshii
    • 4yov, 4yow, 4yox, 4yoy – PhExN phoexo I (mutant) + DNA
    • 4qoz, 4l8r – hExN + histone RNA hairpin-binding protein + RNA
  • 5’-3’ ExN
  • ExN Trex
    • 1y97 – hExN Trex2
    • 2o4g - mExN Trex1 + nucleotide – mouse
    • 3mxj - mExN Trex1
    • 2o4i, 3mxi, 3mxm, 3u3y, 3u6f - mExN Trex1 (mutant) + polynucleotide
    • 2oa8 - mExN Trex1 + DNA
    • 4ynq - mExN Trex1 (mutant) + DNA
    • 3b6o, 3b6p - mExN Trex1 + ion inhibitor
  • Other ExN
    • 1ir6, 2zxo, 2zxp, 2zxr – ExN Recj – Thermus thermophiles
    • 1w0h – hExn Eri1 nuclease domain
    • 1zbu - hExn Eri1
    • 1zbh - hExn Eri1 (mutant) + DNA
    • 5aho – hExN Apollo
    • 2w45 – H4ExN alkaline - Herpesvirus 4
    • 2w4b - H4ExN alkaline (mutant)
    • 3syy - LhExN alkaline – Laribacter hongkongensis
    • 3sz4 - LhExN alkaline + AMP
    • 3sz5 - LhExN alkaline + polynucleotide
    • 3e2v – yExN
    • 4lty, 4lu9, 4m0v – EcExN sbcD

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ReferencesReferences

  1. Mukherjee D, Fritz DT, Kilpatrick WJ, Gao M, Wilusz J. Analysis of RNA exonucleolytic activities in cellular extracts. Methods Mol Biol. 2004;257:193-212. PMID:14770007 doi:http://dx.doi.org/10.1385/1-59259-750-5:193
  2. Breyer WA, Matthews BW. Structure of Escherichia coli exonuclease I suggests how processivity is achieved. Nat Struct Biol. 2000 Dec;7(12):1125-8. PMID:11101894 doi:10.1038/81978

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