ArticleMolecular and cellular biology1997
PRH75, a new nucleus-localized member of the DEAD-box protein family from higher plants.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 38 citations in OpenAlex.
- The nuclear GUCT domain-containing DEAD-box RNA helicases govern gametophytic and sporophytic development in Physcomitrium patens.Plant molecular biology · 2021Article
- MicroRNAs expression dynamics reveal post-transcriptional mechanisms regulating seed development in Phaseolus vulgaris L.Horticulture research · 2021Article
- An Arabidopsis ATP-dependent, DEAD-box RNA helicase loses activity upon IsoAsp formation but is restored by PROTEIN ISOASPARTYL METHYLTRANSFERASE.The Plant cell · 2013Article
- Chloroplast RH3 DEAD box RNA helicases in maize and Arabidopsis function in splicing of specific group II introns and affect chloroplast ribosome biogenesis.Plant physiology · 2012Article
- Gene expression profiling through microarray analysis in Arabidopsis thaliana colonized by Pseudomonas putida MTCC5279, a plant growth promoting rhizobacterium.Plant signaling & behavior · 2012Article
- Substrates of the Arabidopsis thaliana protein isoaspartyl methyltransferase 1 identified using phage display and biopanning.The Journal of biological chemistry · 2010Article
- The DEAD-box protein PMH2 is required for efficient group II intron splicing in mitochondria of Arabidopsis thaliana.Plant molecular biology · 2010Article
- SPIN1, a K homology domain protein negatively regulated and ubiquitinated by the E3 ubiquitin ligase SPL11, is involved in flowering time control in rice.The Plant cell · 2008Article
- Two DEAD-box proteins may be part of RNA-dependent high-molecular-mass protein complexes in Arabidopsis mitochondria.Plant physiology · 2007Article
- Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA.Biochemistry · 2007Article
- Use of fluorescent protein tags to study nuclear organization of the spliceosomal machinery in transiently transformed living plant cells.Molecular biology of the cell · 2004Article
- RNA helicase-like protein as an early regulator of transcription factors for plant chilling and freezing tolerance.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Cloning and characterization of a DEAD box RNA helicase from the viable seedlings of aged mung bean.Plant molecular biology · 2001Article
- Characterization of the cold stress-induced cyanobacterial DEAD-box protein CrhC as an RNA helicase.Nucleic acids research · 2000Article
- Hepatitis C virus core protein interacts with cellular putative RNA helicase.Journal of virology · 1999Article
- Characterization of a DEAD box ATPase/RNA helicase protein of Arabidopsis thaliana.Nucleic acids research · 1998Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The putative RNA helicases of the DEAD-box protein family are involved in pre-mRNA splicing, rRNA maturation, ribosome assembly, and translation. Members of this protein family have been identified in organisms from Escherichia coli to humans, but except for the translation initiation factor 4A, there have been no reports on the characterization of other DEAD-box proteins from plants. Here we report on a novel member of the DEAD-box protein family, the plant RNA helicase 75 (PRH75). PRH75 is localized in the nucleus and contains two domains for RNA binding. One is located at the C terminus and is similar to RGG RNA-binding domains of nucleus-localized RNA-binding proteins. The other one is located between amino acids 308 and 622, a region containing the conserved motif VI characteristic of DEAD-box proteins and known as the RNA-binding site of eIF-4A. The N-terminal 81 amino acids are sufficient for nuclear targeting of the protein. Northern and Western blot analyses show that PRH75 is mainly expressed in young and rapidly developing tissues. The purified recombinant PRH75 has a weak ATPase activity which is barely stimulated by RNA ligands. The fractionation of spinach whole-cell extracts by glycerol gradient centrifugation and gel filtration on a Superdex 200 column shows that the protein exists in a complex of about 500 kDa. Possible biological functions of PRH75 as well as structure-function relationships in the context of its modular primary structure are discussed.
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