Overlapping in short motif sequences for binding to human REV7 and MAD2 proteins

Tomo Hanafusa, Toshiyuki Habu, Junya Tomida, Eiji Ohashi, Yoshiki Murakumo, Haruo Ohmori

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)


Polζ, a DNA polymerase specialized for translesion DNA synthesis (TLS), is comprised of two subunits, the REV3 catalytic subunit and the REV7 accessory subunit. The human REV7 (hREV7) protein is known to interact with hREV3, hREV1 (another TLS protein) and some other proteins such as ADAM9 (a disintegrin and metalloprotease) and ELK-1 (an Ets-like transcription factor). hREV7 is alternatively termed hMAD2L2, because its primary sequence shows 26% identity to that of hMAD2 that plays crucial roles in spindle assembly checkpoint (SAC) via interactions with hMAD1 or hCDC20. Here, we have investigated the molecular basis for the interactions of hREV7/MAD2L2 and hMAD2 with their binding partners. Our results showed that a short sequence of hREV3 is necessary and sufficient for interaction with hREV7. Surprisingly, hMAD2 also binds to the hREV7-binding sequence in hREV3, whereas hMAD2 does not bind to a similar sequence in ADAM9 or ELK-1 and hREV7 does not bind to the hMAD2-binding sequence in hMAD1 or hCDC20. We discuss how hREV7 and hMAD2 recognize their binding partners, and how hREV3 and hREV7 might be involved in SAC.

Original languageEnglish
Pages (from-to)281-296
Number of pages16
JournalGenes to Cells
Issue number3
Publication statusPublished - Mar 2010

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology


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