ArticleNucleic acids research1999
Isolation and characterisation of the cDNA encoding a glycosylated accessory protein of pea chloroplast DNA polymerase.
Article in Nucleic acids research, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 24 citations in OpenAlex.
- Plant plastids: from evolutionary origins to functional specialization and organelle interactions.Journal of experimental botany · 2025Review
- Post-translational Modifications in Regulation of Chloroplast Function: Recent Advances.Frontiers in plant science · 2017Review
- Article
- Posttranslational Modifications of Chloroplast Proteins: An Emerging Field.Plant physiology · 2015Review
- A comparative study of lectin affinity based plant N-glycoproteome profiling using tomato fruit as a model.Molecular & cellular proteomics : MCP · 2014Article
- The rice alpha-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids.The Plant cell · 2009Article
- An S-RNase-based gametophytic self-incompatibility system evolved only once in eudicots.Journal of molecular evolution · 2008Article
- Evolutionary relationships among self-incompatibility RNases.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cDNA encoding p43, a DNA binding protein from pea chloroplasts (ct) that binds to cognate DNA polymerase and stimulates the polymerase activity, has been cloned and characterised. The characteristic sequence motifs of hydroxyproline-rich glyco-proteins (HRGP) are present in the cDNA corres-ponding to the N-terminal domain of the mature p43. The protein was found to be highly O-arabinosylated. Chemically deglycosylated p43 (i.e. p29) retains its binding to both DNA and pea ct-DNA polymerase but fails to stimulate the DNA polymerase activity. The mature p43 is synthesised as a pre-p43 protein containing a 59 amino acid long transit peptide which undergoes stromal cleavage as evidenced from the post-translational in vitro import of the precursor protein into the isolated intact pea chloroplasts. Surprisingly, p43 is found only in pea chloroplasts. The unique features present in the cloned cDNA indicate that p43 is a novel member of the HRGP family of proteins. Besides p43, no other DNA-polymerase accessory protein with O-glycosylation has been reported yet.
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