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Rif1 is a large multifaceted protein involved in various processes of DNA metabolism – from telomere length regulation and replication to double-strand break repair. The mechanistic details of its action, however, are often poorly understood. Here, we report functional characterization of the Rif1 homologue from methylotrophic thermotolerant budding yeast  Hansenula polymorpha  DL-1. We show that, similar to other yeast species,  H. polymorpha  Rif1 suppresses telomerase-dependent telomere elongation. We uncover two novel modes of Rif1 recruitment at  H. polymorpha  telomeres: via direct DNA binding and through the association with the Ku heterodimer. Both of these modes (at least partially) require the intrinsically disordered N-terminal extension – a region of the protein present exclusively in yeast species. We also demonstrate that Rif1 binds Stn1 and promotes its accumulation at telomeres in  H. polymorpha .

Telomere length regulation by Rif1 protein from Hansenula polymorpha