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Literature summary for 2.7.7.B22 extracted from

  • Choi, K.Y.; Spencer, J.M.; Craig, N.L.
    The Tn7 transposition regulator TnsC interacts with the transposase subunit TnsB and target selector TnsD (2014), Proc. Natl. Acad. Sci. USA, 111, E2858-E2865.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.B22

Cloned(Commentary)

Cloned (Comment) Organism
genes tnsABCDE, recombinant expression in Escherichia coli strain ER2566 from an pCYB1 intein vector, recombinant expression of TnsC1-85 as MBP-fusion protein in Escherichia coli strain BL21Star(DE3) pET101/DTOPO-TnsD1-309His Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of diverse truncation mutants of TnsB, TnsC, and TnsD, and of double-mutant MBP-TnsC361–555 P468A/L470A Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P13988 AND P13989 tnsA and tnsB
-

Purification (Commentary)

Purification (Comment) Organism
recombinant TnsC1-85 MBP-fusion protein from Escherichia coli strain BL21Star(DE3) pET101/DTOPO-TnsD1–309His, co-purification of the TnsC and TnsD fragments by nickel affinity chromatography, TnsC1-85 interacts directly with TnsD1-309 Escherichia coli

Subunits

Subunits Comment Organism
More trypsin peptide mapping of TnsC Escherichia coli

Synonyms

Synonyms Comment Organism
Tn7 transposase
-
 Escherichia coli
TnsA
-
 Escherichia coli
TnsB
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Escherichia coli

General Information

General Information Comment Organism
malfunction a TnsC mutant defective in interaction with TnsB is defective for Tn7 transposition both in vitro and in vivo Escherichia coli
metabolism DNA cut-and-paste transposons are discrete DNA segments that move from place to place within genomes via excision from a donor site by double-strand DNA breaks and insertion into a target site. These events are mediated by nucleoprotein complexes whose assembly regulates and coordinates breakage and joining. Multiple protein-protein and protein-DNA interactions are involved in assembly of these nucleoprotein complexes Escherichia coli
physiological function the excision of transposon Tn7 from a donor site and its insertion into its preferred target site, attachment site attTn7, is mediated by four Tn7-encoded transposition proteins: TnsA, TnsB, TnsC, and TnsD. Transposition requires the assembly of a nucleoprotein complex containing all four Tns proteins and the DNA substrates, the donor site containing Tn7, and the preferred target site attTn7. TnsA and TnsB together form the heteromeric Tn7 transposase, and TnsD is a target-selecting protein that binds specifically to attTn7. TnsC is the key regulator of transposition, interacting with both the TnsAB transposase and TnsD-attTn7. TnsC interacts directly with TnsB via its C-terminus, identification of the specific region of TnsC involved in the TnsB-TnsC interaction during transposition. TnsC amino acids L475 and L476 play important roles in the interaction of the peptide TnsB with TnsC. Tn7 displays cis-acting target immunity, which blocks Tn7 insertion into a target DNA that already contains Tn7, the direct TnsB-TnsC interaction also mediates cis-acting Tn7 target immunity. TnsC also interacts directly with the target selector protein TnsD, TnsC and TnsD together form a complex with the transposon attachment site attTn7. Interaction analysis, overview Escherichia coli