{"title":"Sub2: A TFIIB Interacting Protein with Pleiotropic Roles in mRNA Synthesis, Processing and Transport.","authors":"E Fidler, A Ansari","doi":"10.23880/ijbp-16000250","DOIUrl":"10.23880/ijbp-16000250","url":null,"abstract":"<p><p>The generally accepted view is that different steps of transcription, mRNA processing and mRNA trafficking are performed by dedicated accessory factors. The research during last couple of decades, however, has challenged this dogma. We recently showed that the general transcription factor TFIIB, in addition to its well established role in initiation, is also involved in termination of transcription. Mass spectrometry of purified TFIIB revealed Sub2 as one of its major interacting partners. Sub2 has already been implicated in elongation step of transcription, splicing and mRNA trafficking. Interaction of Sub2 with TFIIB implicates it in initiation and termination steps of transcription. Multiplicity of Sub2 biological roles may be responsible for its link with a number of human pathological conditions making it a potential drug target.</p>","PeriodicalId":520017,"journal":{"name":"International journal of biochemistry & physiology","volume":"9 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12055297/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144035170","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Fibrinogen in Hamster Cauda Sperm.","authors":"T Salters, B Sharpe, S S Raychoudhury, S K Nagdas","doi":"10.23880/ijbp-16000237","DOIUrl":"10.23880/ijbp-16000237","url":null,"abstract":"<p><p>Epididymis plays a vital role in promoting sperm maturation and maintaining sperm viability. It has been shown the presence of nonviable sperm in cauda epididymis. We previously identified a secretory protein (260/280KDa oligomers) of hamster cauda epididymal principal cells that binds to nonviable sperm. The 260/280KDa oligomers are composed of 64kDa FGL2 (fibrinogen-like protein-2) and 33kDa FGL1) (fibrinogen-like protein-1). In addition, we have demonstrated that FGL2 is a phospholipid-activated serine protease; the conversion of prothrombin to thrombin by FGL2 followed by the conversion of soluble fibrinogen to insoluble fibrin polymers by thrombin. In the present study, we have shown the presence of a 56kDa fibrinogen β in hamster cauda sperm. The potential role of fibrinogen in hamster physiology is being discussed.</p>","PeriodicalId":520017,"journal":{"name":"International journal of biochemistry & physiology","volume":"8 2","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11323058/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141984279","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}