Fig. 2: Bmc1 interacts with the same TER1 species as well-established components of the telomerase holoenzyme. | Nature Communications

Fig. 2: Bmc1 interacts with the same TER1 species as well-established components of the telomerase holoenzyme.

From: The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme

Fig. 2

A The 5’ and 3’ ends of Bmc1-, Trt1-, Pof8-, and Lsm3-associated TER1 were identified by cRACE. The results of ten independent clones per immunoprecipitation are shown below a schematic of the architecture of TER1. B RNase H northern blots of RNase H-generated 5’ and 3’ ends of TER1 immunoprecipitated by various telomerase components. The same blot was stripped and reprobed for U6. C, D Northern blot of α-TMG flow through (FT) and immunoprecipitated (IP) transcripts from total RNA (C) and Bmc1-associated RNA (D). Source data are provided as a Source Data file.

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