ライフサイエンスコーパス: colicin E1

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1 inal pore-forming domain of the bacteriocin, colicin E1.

2 channel-forming activity of the bacteriocin, colicin E1.

3 ile its absence renders the cell tolerant to colicin E1.

4 bility of cobalamin to inhibit the action of colicin E1.

5 In contrast, for colicin E1 action on TolA delta3 cells, there was little

6 unter-selection escape by 425-fold, compared colicin E1 alone.

7 Colicins E1 and E3 initially bind to the BtuB receptor,

8 ers with the same orientation constraints as colicins E1 and E3.

9 action and unique translocation mechanism of colicin E1 are discussed.

10 Upon binding to membranes, the 178-residue colicin E1 C-terminal channel protein forms a steady-sta

11 urrent and the conformational flexibility of colicin E1 channel domain depend on the membrane surface

12 urther support for the umbrella model of the colicin E1 channel domain.

13 In vitro channel activity of the C-terminal colicin E1 channel polypeptide under conditions of varia

14 Data suggest a two-receptor model for colicin E1 (ColE1) translocation across the outer membra

15 s explored by interchanging residues between colicins E1 (ColE1) and 10 (Col10) and testing for alter

16 d for the translocation of group A colicins (colicins E1, E2, E3, A, K, and N) across the cell envelo

17 The colicin E1 immunity protein (ImmE1), a 13.2-kDa hydropho

18 It was concluded that the colicin E1 immunity protein adopts a folded conformation

19 nvolvement of overlapping regions of TolC in colicin E1 import and phage binding.The phage used in th

20 itate the entry of the bacteriophage TLS and colicin E1 into the bacterial cell.

21 The channel-forming domain of colicin E1 is composed of a soluble helical bundle which

22 The synthesis of colicin E1 is known to be regulated by the SOS response,

23 the mechanism(s) by which cellular uptake of colicin E1 is mediated by the TolA protein differs from

24 colicin fragment and the 522 residue intact colicin E1 molecule scale qualitatively according to the

25 f the loops were essential for the action of colicin E1 or E3, which is consistent with the crystallo

26 -terminal 190-residue channel polypeptide of colicin E1 (P190) bound to anionic membranes are describ

27 but counter-selection escape frequency using colicin E1 precludes using tolC for inefficient genetic

28 ants showed varying degrees of resistance to colicin E1, suggesting the involvement of overlapping re

29 of denaturation profiles of the 522 residue colicin E1, together with fragments of 342 and 178 resid

30 (Val(447)-Gly(475) and Ile(508)-Ile(522)) of colicin E1 was investigated by a site-directed fluoresce

31 ty, and structure of the toxin-like molecule colicin E1 were analyzed by differential scanning calori

32 s E3 and N, and the TolC recognition site of colicin E1, were found to reside in the N-terminal trans

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