scholarly journals Pre-Messenger RNA Processing Factors in the Drosophila Genome

2000 ◽  
Vol 150 (2) ◽  
pp. F37-F44 ◽  
Author(s):  
Stephen M. Mount ◽  
Helen K. Salz
Author(s):  
Sarah Schleicher ◽  
Stefan Binder

Abstract Key message RNA PROCESSING FACTORs 1 AND 8 (RPF1 and RPF8), both restorer of fertility like pentatricopeptide repeat proteins, are required for processing of dicistronic nad4L-atp4 and nad3-rps12 transcripts in Arabidopsis mitochondria. Abstract In mitochondria of Arabidopsis thaliana (Arabidopsis), the 5′ termini of many RNAs are generated on the post-transcriptional level. This process is still poorly understood in terms of both the underlying mechanism as well as proteins required. Our studies now link the generation of polymorphic 5′ extremities of the dicistronic nad3-rps12 and nad4L-atp4 transcripts to the function of the P-type pentatricopeptide repeat proteins RNA PROCESSING FACTORs 8 (RPF8) and 1 (RPF1). RPF8 is required to generate the nad3-rps12 -141 5′ end in ecotype Van-0 whereas the RPF8 allele in Col has no function in the generation of any 5′ terminus of this transcript. This observation strongly suggests the involvement of an additional factor in the generation of the -229 5′ end of nad3-rps12 transcripts in Col. RPF1, previously found to be necessary for the generation of the -228 5′ end of the major 1538 nucleotide-long nad4 mRNAs, is also important for the formation of nad4L-atp4 transcripts with a 5′ end at position -318 in Col. Many Arabidopsis ecotypes contain inactive RPF1 alleles resulting in the accumulation of various low abundant nad4L-atp4 RNAs which might represent precursor and/or degradation products. Some of these ecotypes accumulate major, but slightly smaller RNA species. The introduction of RPF1 into these lines not only establishes the formation of the major nad4L-atp4 dicistronic mRNA with the -318 5′ terminus, the presence of this gene also suppresses the accumulation of most alternative nad4L-atp4 RNAs. Beside RPF1, several other factors contribute to nad4L-atp4 transcript formation.


2000 ◽  
Vol 129 (2-3) ◽  
pp. 241-251 ◽  
Author(s):  
Paul J. Mintz ◽  
David L. Spector

2006 ◽  
Vol 66 (9) ◽  
pp. 4561-4565 ◽  
Author(s):  
Ho-Shik Kim ◽  
Hongjie Li ◽  
Murat Cevher ◽  
Alissa Parmelee ◽  
Danae Fonseca ◽  
...  

2009 ◽  
Vol 395 (2) ◽  
pp. 237-243 ◽  
Author(s):  
Ayan Banerjee ◽  
Mimi C. Sammarco ◽  
Scott Ditch ◽  
Ed Grabczyk

Author(s):  
K. Potter ◽  
N. Cremona ◽  
J.A. Wise
Keyword(s):  

2016 ◽  
Vol 213 (5) ◽  
pp. 557-570 ◽  
Author(s):  
Deirdre C. Tatomer ◽  
Esteban Terzo ◽  
Kaitlin P. Curry ◽  
Harmony Salzler ◽  
Ivan Sabath ◽  
...  

The histone locus body (HLB) assembles at replication-dependent histone genes and concentrates factors required for histone messenger RNA (mRNA) biosynthesis. FLASH (Flice-associated huge protein) and U7 small nuclear RNP (snRNP) are HLB components that participate in 3′ processing of the nonpolyadenylated histone mRNAs by recruiting the endonuclease CPSF-73 to histone pre-mRNA. Using transgenes to complement a FLASH mutant, we show that distinct domains of FLASH involved in U7 snRNP binding, histone pre-mRNA cleavage, and HLB localization are all required for proper FLASH function in vivo. By genetically manipulating HLB composition using mutations in FLASH, mutations in the HLB assembly factor Mxc, or depletion of the variant histone H2aV, we find that failure to concentrate FLASH and/or U7 snRNP in the HLB impairs histone pre-mRNA processing. This failure results in accumulation of small amounts of polyadenylated histone mRNA and nascent read-through transcripts at the histone locus. Thus, the HLB concentrates FLASH and U7 snRNP, promoting efficient histone mRNA biosynthesis and coupling 3′ end processing with transcription termination.


1983 ◽  
Vol 97 (5) ◽  
pp. 1321-1326 ◽  
Author(s):  
T Pederson

Eucaryotic messenger RNA precursors are processed in nuclear ribonucleoprotein particles (hnRNP). Here recent work on the structure of hnRNP is reviewed, with emphasis on function. Detailed analysis of a specific case, the altered assembly of hnRNP in heat-shocked Drosophila and mammalian cells, leads to a general hypothesis linking hnRNP structure and messenger RNA processing.


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