ArticleNucleic acids research2011
Determinants of Nam8-dependent splicing of meiotic pre-mRNAs.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- The U1 snRNP component RBP45d regulates temperature-responsive flowering in Arabidopsis.The Plant cell · 2022Article
- A genetic screen in Arabidopsis reveals the identical roles for RBP45d and PRP39a in 5' cryptic splice site selection.Frontiers in plant science · 2022Article
- Principles and correction of 5'-splice site selection.RNA biology · 2022Review
- The SR-protein Npl3 is an essential component of the meiotic splicing regulatory network in Saccharomyces cerevisiae.Nucleic acids research · 2021Article
- Mutagenesis of Snu114 domain IV identifies a developmental role in meiotic splicing.RNA biology · 2019Article
- Domain Requirements and Genetic Interactions of the Mud1 Subunit of theG3 (Bethesda, Md.) · 2019Article
- Pre-mRNA Splicing in the Nuclear Landscape.Cold Spring Harbor symposia on quantitative biology · 2019Article
- CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing.Nature communications · 2017Article
- The chromatin remodeling complex Swi/Snf regulates splicing of meiotic transcripts in Saccharomyces cerevisiae.Nucleic acids research · 2017Article
- Structural basis for recognition of intron branchpoint RNA by yeast Msl5 and selective effects of interfacial mutations on splicing of yeast pre-mRNAs.RNA (New York, N.Y.) · 2015Article
- Structure-function analysis of the Yhc1 subunit of yeast U1 snRNP and genetic interactions of Yhc1 with Mud2, Nam8, Mud1, Tgs1, U1 snRNA, SmD3 and Prp28.Nucleic acids research · 2014Article
- Structure-function analysis of the 5' end of yeast U1 snRNA highlights genetic interactions with the Msl5*Mud2 branchpoint-binding complex and other spliceosome assembly factors.Nucleic acids research · 2013Article
- Genetic interactions of hypomorphic mutations in the m7G cap-binding pocket of yeast nuclear cap binding complex: an essential role for Cbc2 in meiosis via splicing of MER3 pre-mRNA.RNA (New York, N.Y.) · 2012Article
- Structure-function analysis and genetic interactions of the yeast branchpoint binding protein Msl5.Nucleic acids research · 2012Article
- Cwc24p is a general Saccharomyces cerevisiae splicing factor required for the stable U2 snRNP binding to primary transcripts.PloS one · 2012Article
- Functional consequences of developmentally regulated alternative splicing.Nature reviews. Genetics · 2011Review
- Defining the Mer1 and Nam8 meiotic splicing regulons by cDNA rescue.RNA (New York, N.Y.) · 2011Article
- Composition of yeast snRNPs and snoRNPs in the absence of trimethylguanosine caps reveals nuclear cap binding protein as a gained U1 component implicated in the cold-sensitivity of tgs1Δ cells.Nucleic acids research · 2011Article
- An essential role for trimethylguanosine RNA caps in Saccharomyces cerevisiae meiosis and their requirement for splicing of SAE3 and PCH2 meiotic pre-mRNAs.Nucleic acids research · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Nam8, a component of yeast U1 snRNP, is optional for mitotic growth but required during meiosis, because Nam8 collaborates with Mer1 to promote splicing of essential meiotic mRNAs AMA1, MER2 and MER3. Here, we identify SPO22 and PCH2 as novel targets of Nam8-dependent meiotic splicing. Whereas SPO22 splicing is co-dependent on Mer1, PCH2 is not. The SPO22 intron has a non-consensus 5' splice site (5'SS) that dictates its Nam8/Mer1-dependence. SPO22 splicing relies on Mer1 recognition, via its KH domain, of an intronic enhancer 5'-AYACCCUY. Mutagenesis of KH and the enhancer highlights Arg214 and Gln243 and the CCC triplet as essential for Mer1 activity. The Nam8-dependent PCH2 pre-mRNA has a consensus 5'SS and lacks a Mer1 enhancer. For PCH2, a long 5' exon and a non-consensus intron branchpoint dictate Nam8-dependence. Our results implicate Nam8 in two distinct meiotic splicing regulons. Nam8 is composed of three RRM domains, flanked by N-terminal leader and C-terminal tail segments. The leader, tail and RRM1 are dispensable for splicing meiotic targets and unnecessary for vegetative Nam8 function in multiple synthetic lethal genetic backgrounds. Nam8 activity is enfeebled by alanine mutations in the putative RNA binding sites of the RRM2 and RRM3 domains.
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