PubMed:22905263 / 843-1657 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/22905263","sourcedb":"PubMed","sourceid":"22905263","source_url":"https://www.ncbi.nlm.nih.gov/pubmed/22905263","text":"We find that Mos1 transposase concentrations in excess to the Mos1 ends prevent the paired-end complex assembly. However, we observe that Mos1 transposition is not impaired by transposase high concentration, dismissing the idea that transposase over production plays an obligatory role in the down-regulation of mariner transposition. Our main finding is that the paired-end complex is formed in a cooperative way, regardless of the transposase concentration. We also show that an element framed by two identical ITRs (Inverted Terminal Repeats) is more efficient in driving transposition than an element framed by two different ITRs (i.e. the natural Mos1 copy), the latter being more sensitive to transposase concentration variations. Finally, we show that the current Mos1 ITRs correspond to the ancestral ones.","tracks":[{"project":"PubMed_Structured_Abstracts","denotations":[{"id":"T2","span":{"begin":0,"end":814},"obj":"RESULTS"}],"attributes":[{"subj":"T2","pred":"source","obj":"PubMed_Structured_Abstracts"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"PubMed_Structured_Abstracts","color":"#93b3ec","default":true}]}]}}