The process of transcriptional elongation by RNA polymerase II (RNAPII) in a chromatin context involves a large number of crucial factors. SPN1 is a highly conserved protein encoded by an essential gene and is known to interact with RNAPII and the histone chaperone SPT6. SPN1 negatively regulates the ability of SPT6 to interact with nucleosomes, but the chromatin binding properties of SPN1 are largely unknown. Here, we demonstrate that full length SPN1 (amino acids 1-410) binds DNA, histones H3-H4, mononucleosomes and nucleosomal arrays, and has weak nucleosome assembly activity. The core domain of SPN1 (amino acids 141-305), which is necessary and sufficient in Saccharomyces cerevisiae for growth under ideal growth conditions, is unable to optimally interact with histones, nucleosomes and/or DNA and fails to assemble nucleosomes in vitro. Although competent for binding with SPT6 and RNAPII, the core domain derivative is not stably recruited to the CYC1 promoter, indicating chromatin interactions are an important aspect of normal SPN1 functions in vivo. Moreover, strong synthetic genetic interactions are observed with SPN1 mutants and deletions of histone chaperone genes. Taken together, these results indicate that SPN1 is a histone binding factor with histone chaperone functions.

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Journal Article | Research Support, N.I.H., Extramural | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, Non-P.H.S.

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Li S, Almeida AR, Radebaugh CA, Zhang L, Chen X, Huang L, Thurston AK, Kalashnikova AA, Hansen JC, Luger K, ... Show all

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