{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Skrajna A"],"funding":["CEPT","NIH","NIGMS NIH HHS"],"pagination":["1180-1196"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4847949"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["428(6)"],"pubmed_abstract":["Histone pre-mRNAs are cleaved at the 3' end by a complex that contains U7 snRNP, the FLICE-associated huge protein (FLASH) and histone pre-mRNA cleavage complex (HCC) consisting of several polyadenylation factors. Within the complex, the N terminus of FLASH interacts with the N terminus of the U7 snRNP protein Lsm11, and together they recruit the HCC. FLASH through its distant C terminus independently interacts with the C-terminal SANT/Myb-like domain of nuclear protein, ataxia-telangiectasia locus (NPAT), a transcriptional co-activator required for expression of histone genes in S phase. To gain structural information on these interactions, we used mass spectrometry to monitor hydrogen/deuterium exchange in various regions of FLASH, Lsm11 and NPAT alone or in the presence of their respect"],"journal":["Journal of molecular biology"],"pubmed_title":["Mapping the Interaction Network of Key Proteins Involved in Histone mRNA Generation: A Hydrogen/Deuterium Exchange Study."],"pmcid":["PMC4847949"],"funding_grant_id":["GM29832","POIG.02.02.00-00-025/09","R01 GM029832"],"pubmed_authors":["Marzluff WF","Skrajna A","Yang XC","Dadlez M","Fituch K","Dominski Z","Tarnowski K"],"additional_accession":[]},"is_claimable":false,"name":"Mapping the Interaction Network of Key Proteins Involved in Histone mRNA Generation: A Hydrogen/Deuterium Exchange Study.","description":"Histone pre-mRNAs are cleaved at the 3' end by a complex that contains U7 snRNP, the FLICE-associated huge protein (FLASH) and histone pre-mRNA cleavage complex (HCC) consisting of several polyadenylation factors. Within the complex, the N terminus of FLASH interacts with the N terminus of the U7 snRNP protein Lsm11, and together they recruit the HCC. FLASH through its distant C terminus independently interacts with the C-terminal SANT/Myb-like domain of nuclear protein, ataxia-telangiectasia locus (NPAT), a transcriptional co-activator required for expression of histone genes in S phase. To gain structural information on these interactions, we used mass spectrometry to monitor hydrogen/deuterium exchange in various regions of FLASH, Lsm11 and NPAT alone or in the presence of their respect","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Mar","modification":"2025-04-04T02:23:47.511Z","creation":"2019-03-27T02:12:33Z"},"accession":"S-EPMC4847949","cross_references":{"pubmed":["26860583"],"doi":["10.1016/j.jmb.2016.01.031"]}}