The authors would like to make the following corrections to this published paper [
1].
Upon reviewing
Figure 3C (lane Y230), the authors observed a formatting error in the blot. Thus,
Figure 3 should be replaced with the following version:
Figure 3.
UV crosslinking reveals that ICP22 interacts directly with the FACT complex. (A) Amino-acid sequence of ICP22 showing the positions at which a TAG stop codon is introduced and Bpa is incorporated within ICP22; (B) HEK293 cells were co-transfected with wild-type ICP22 cDNA (WT) or ICP22 cDNA with a TAG stop codon replacing different amino acid codons (represented by the asterisk) and suppressor tRNA/Bpa synthetase pair in the absence or presence of photo-cross-linkable Bpa. Flag immunoprecipitation was performed from total cell extracts and separated by SDS-PAGE. Western blots were probed with an anti-Flag antibody; (C) Flag immunoprecipitation of ICP22Bpa from cell extracts after cells were UV irradiated alive (+) in chilled PBS or not (−). Western blot was probed with an anti-Flag antibody; (D) HEK293 cells were co-transfected with ICP22 cDNA with a TAG stop codon replacing Y230 and suppressor tRNA/Bpa synthetase pair in the presence of photo-cross-linkable Bpa, and UV-irradiated alive (+) in ice-cold PBS. Flag immunoprecipitation was performed from total cell extracts, cytoplasmic and nuclear fractions and separated by SDS-PAGE. Western blots were probed with antibodies against Flag and FACT complex subunits SPT16 and SSRP1; (E) HEK293 cells were co-transfected with ICP22 cDNA with a TAG stop codon replacing L191 or C225 and suppressor tRNA/Bpa synthetase pair in the presence of photo-cross-linkable Bpa, and UV-irradiated alive (+) in ice-cold PBS. Flag immunoprecipitation was performed from total cell extracts and separated by SDS-PAGE. Western blots were probed with antibodies against Flag and FACT complex subunits SPT16 and SSRP1.
Figure 3.
UV crosslinking reveals that ICP22 interacts directly with the FACT complex. (A) Amino-acid sequence of ICP22 showing the positions at which a TAG stop codon is introduced and Bpa is incorporated within ICP22; (B) HEK293 cells were co-transfected with wild-type ICP22 cDNA (WT) or ICP22 cDNA with a TAG stop codon replacing different amino acid codons (represented by the asterisk) and suppressor tRNA/Bpa synthetase pair in the absence or presence of photo-cross-linkable Bpa. Flag immunoprecipitation was performed from total cell extracts and separated by SDS-PAGE. Western blots were probed with an anti-Flag antibody; (C) Flag immunoprecipitation of ICP22Bpa from cell extracts after cells were UV irradiated alive (+) in chilled PBS or not (−). Western blot was probed with an anti-Flag antibody; (D) HEK293 cells were co-transfected with ICP22 cDNA with a TAG stop codon replacing Y230 and suppressor tRNA/Bpa synthetase pair in the presence of photo-cross-linkable Bpa, and UV-irradiated alive (+) in ice-cold PBS. Flag immunoprecipitation was performed from total cell extracts, cytoplasmic and nuclear fractions and separated by SDS-PAGE. Western blots were probed with antibodies against Flag and FACT complex subunits SPT16 and SSRP1; (E) HEK293 cells were co-transfected with ICP22 cDNA with a TAG stop codon replacing L191 or C225 and suppressor tRNA/Bpa synthetase pair in the presence of photo-cross-linkable Bpa, and UV-irradiated alive (+) in ice-cold PBS. Flag immunoprecipitation was performed from total cell extracts and separated by SDS-PAGE. Western blots were probed with antibodies against Flag and FACT complex subunits SPT16 and SSRP1.
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The authors apologize for any inconvenience this may have caused and affirm that the scientific conclusions remain unaffected. The original publication has also been updated.