<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Skrajna A</submitter><funding>CEPT</funding><funding>NIH</funding><funding>NIGMS NIH HHS</funding><pagination>1180-1196</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4847949</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>428(6)</volume><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</pubmed_abstract><journal>Journal of molecular biology</journal><pubmed_title>Mapping the Interaction Network of Key Proteins Involved in Histone mRNA Generation: A Hydrogen/Deuterium Exchange Study.</pubmed_title><pmcid>PMC4847949</pmcid><funding_grant_id>GM29832</funding_grant_id><funding_grant_id>POIG.02.02.00-00-025/09</funding_grant_id><funding_grant_id>R01 GM029832</funding_grant_id><pubmed_authors>Marzluff WF</pubmed_authors><pubmed_authors>Skrajna A</pubmed_authors><pubmed_authors>Yang XC</pubmed_authors><pubmed_authors>Dadlez M</pubmed_authors><pubmed_authors>Fituch K</pubmed_authors><pubmed_authors>Dominski Z</pubmed_authors><pubmed_authors>Tarnowski K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Mapping the Interaction Network of Key Proteins Involved in Histone mRNA Generation: A Hydrogen/Deuterium Exchange Study.</name><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</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Mar</publication><modification>2025-04-04T02:23:47.511Z</modification><creation>2019-03-27T02:12:33Z</creation></dates><accession>S-EPMC4847949</accession><cross_references><pubmed>26860583</pubmed><doi>10.1016/j.jmb.2016.01.031</doi></cross_references></HashMap>