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Protein homology suggests similarities in histone mRNA processing between humans and slime molds
Author(s) -
Roth Stefen Paul,
Lackey Patrick
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.650.8
Subject(s) - biology , polyadenylation , cleavage and polyadenylation specificity factor , histone , microbiology and biotechnology , genetics , snrnp , rna splicing , messenger rna , gene , rna
Histone mRNA is the only metazoan mRNA that is not polyadenylated. Instead, it ends with a conserved 3′ stem loop that, along with its protein binding partner the stem‐loop binding protein (SLBP), is necessary for processing, export into the cytoplasm, and degradation. These mechanisms are well‐studied in humans, Drosophila , and Xenopus , but they are completely absent in fungi like Saccharomyces cerevisiae . Instead, the histone mRNA in these eukaryotes have traditional 3′ poly(A) tails. Because of this, the evolutionary history of the mechanism of stem‐loop control is not well understood. Recently, bioinformatics work has identified histone mRNA with stem‐loops and proteins that closely resemble SLBP in very simple eukaryotes like Dictyostelium discoideum and Chlamydomonas reinhardtii . This presents us with an opportunity to better understand this evolutionary history. The stem loop and SLBP also play a key role in the recruitment of key processing and cleavage factors including, NPAT, FLASH, the U7 snRNP complex (via the snRNP subunits LSM10 and LSM11), and the histone cleavage complex (HCC) made up of symplekin, CPSF 73 and CPSF 100. Together, these proteins work to efficiently process histone pre – mRNA in lower through higher eukaryotes. We have identified homologs of FLASH, NPAT, symplekin, ZFP100 and LSM11 in Dictyostelium . Together with the previously identified binding domains and well understood polyadenylation proteins, this creates a proto‐HCC complex, through which we can begin to understand how the histone processing and cleavage mechanism in these lower organisms compares to the better‐understood mechanism in metazoans. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .