ArticleNucleic acids research1989
Sequence organization and gene expression of pGD1, a plasmid found in a wild isolate of Dictyostelium.
Article in Nucleic acids research, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- Eukaryotic topoisomerase I-DNA interaction is stabilized by helix curvature.Nucleic acids research · 1991Article
- Regulation of the Discoidin I gamma gene in Dictyostelium discoideum: identification of individual promoter elements mediating induction of transcription and repression by cyclic AMP.Molecular and cellular biology · 1990Article
- The extrachromosomal replication of Dictyostelium plasmid Ddp2 requires a cis-acting element and a plasmid-encoded trans-acting factor.Molecular and cellular biology · 1990Article
- Transcript and sequence analysis of a 5.1 kb contiguous fragment of Dictyostelium discoideum plasmid Ddp1 that contains the origin of replication and codes for several transcripts.Current genetics · 1990Article
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
We have determined the complete nucleotide sequence of pDG1, a plasmid found in a wild isolate of Dictyostelium. The 4439-bp long pDG1 contains only one, 2718-bases-long, open reading frame (ORF) and nearly perfect inverted repeats of 551 bp and 552 bp. Northern-blot analysis showed that only one 2.7-kb poly (A)+ RNA transcript was expressed at a maximum level, 2 h (early aggregation stage) after the onset of development. The expression of this transcript was suppressed by the addition of cAMP. In the upstream region of the ORF, there are several putative consensus sequences, e.g. (1) TGACTTAGAA-AAATT which is a putative site for cleavage by topoisomerase I, and (2) TGACGACA which may be a cAMP-responsive element, found in several genes that are regulated by cAMP at the level of transcription. A possible mechanism of the partitioning of pDG1 into daughter cells is discussed.
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