ライフサイエンスコーパス: cpn60

1 rates to cpn10 is possible in the absence of cpn60.

2 by the equivalent region from the homologous cpn60-1 gene of Rhizobium leguminosarum.

3 le ring form in which both the GroEL and the Cpn60-1 proteins are found.

4 ng precise cross-over points, two regions in Cpn60-1 were defined which appeared to be critical for r

5 can complement for loss of the M. smegmatis cpn60.1 gene.

6 We show that the Cpn60.1 proteins, but not the Cpn60.2 proteins, can comp

7 cyte-stimulating activity of M. tuberculosis Cpn60.1 resides in the monomeric subunit and within this

8 tuberculosis expresses two chaperonins, one (Cpn60.1) dispensable and one (Cpn60.2) essential.

9 uberculosis heat shock protein 60 (Mtbhsp60, Cpn60.1, and Rv3417c) interacts with both TLR2 and TLR4

10 We show here that the Cpn60.2 homologue from Mycobacterium smegmatis also fail

11 However, we also show that the Cpn60.2 proteins from both organisms can replace the ess

12 We investigated the oligomerization of the Cpn60.2 proteins using analytical ultracentrifugation an

13 show that the Cpn60.1 proteins, but not the Cpn60.2 proteins, can complement for loss of the M. smeg

14 peronins, one (Cpn60.1) dispensable and one (Cpn60.2) essential.

15 These results indicate cooperation of Cpn60 and cpSecA1 for proper membrane insertion of Plsp1

16 coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed.

17 The deduced amino acid sequences of GroEL1 (cpn60) and GroES1 (cpn10) were in agreement with N-termi

18 a gene encoding one such protein, chaperonin CPN60, and have characterized its structure and expressi

19 al antibodies were developed to maize HSP70, cpn60, and HSP22.

20 we detected coimmunoprecipitation of IAP100, cpn60, and the imported mature form (S) of precursor.

21 The molecular chaperone cpn60 binds many unfolded proteins and facilitates their

22 her, the binding of a hydrophobic surface to cpn60 can induce further exposure of complementary surfa

23 le 700-kDa complex that co-migrated with the Cpn60 complex before inserting into the membrane.

24 urther exposure of complementary surfaces on cpn60 complexes, thus amplifying interactions available

25 the higher plant chloroplast chaperonin 60 (cpn60) consist of roughly equal amounts of two divergent

26 A flexible region, known to interact with cpn60, extends from the lower rim of the dome.

27 ous interpretation of these data is that the cpn60 gene was transferred from the endosymbiotic ancest

28 heat shock protein 70 and/or chaperonin 60 (cpn60) genes in trichomonads and microsporidia imply tha

29 tates substrate folding when in complex with cpn60 (GroEL in E. coli).

30 Entamoeba histolytica CPN60 has an amino-terminal extension reminiscent of kno

31 his report, we describe a mitochondrial-like cpn60 homolog from the diplomonad parasite Giardia lambl

32 hylogenetic analyses position the G. lamblia cpn60 in a clade that includes mitochondrial and hydroge

33 the exposed hydrophilic face did not bind to cpn60 in either the oxidized or reduced states.

34 Thus, binding to cpn60 is favored by a secondary structure that organizes

35 Western blots reveal that the expression of cpn60 is independent of cellular stress and, except duri

36 Deletion of the first 15 amino acids of CPN60 leads to an accumulation of the truncated protein

37 have been used to probe the question of how cpn60 might recognize such a diverse set of unfolded pro

38 cloned the alpha and beta subunits of the ch-cpn60 of pea (Pisum sativum), expressed them individuall

39 envelope membrane (Toc159), stromal (hsp93, cpn60), or thylakoid (LHCP, OE23) proteins were not incr

40 We show that a Cpn60 protein from the bacterium Rhizobium leguminosarum

41 Bacterial Cpn60 proteins (homologues to the Escherichia coli GroEL

42 (42 degrees C for 4 h), levels of HSP70 and cpn60 proteins did not change significantly.

43 nsduced into strains expressing heterologous Cpn60 proteins, to test for complementation at any tempe

44 at includes mitochondrial and hydrogenosomal cpn60 proteins.

45 E. histolytica organelle housing chaperonin CPN60 represents a mitochondrial remnant.

46 seven housekeeping genes, gltA, gdhB, recA, cpn60, rpoD, gyrB, and gpi, with that of sequence-based

47 he 16S rRNA-encoding gene and chaperonin-60 (cpn60) showed that the plants were infected with phytopl

48 that Aacpn10 has molecular interactions with cpn60 similar to other cpn10s.

49 pathogen in Mexico, we designed an array of cpn60-targeted molecular diagnostic assays for SbGP/MPV

50 100 was identified as stromal chaperonin 60 (cpn60); the association of IAP100 and cpn60 was specific

51 ein, we have localized native E. histolytica CPN60 to a previously undescribed organelle of putative

52 o attach to the corresponding chaperonin 60 (cpn60) to enclose unfolded protein and to facilitate its

53 molecular chaperones DnaK (HSP70) and GroEL (cpn60) using two-dimensional sodium dodecyl sulfate-poly

54 ferentiating it from other known phytoplasma cpn60 UT sequences, while identifying a double infection

55 in 60 (cpn60); the association of IAP100 and cpn60 was specific and was abolished when immunoprecipit

56 duce the exposure of hydrophobic surfaces on cpn60, whereas the same peptide in its random coil form

57 Kd = approximately 106 microM for binding to cpn60, whereas there was no detectable binding of the re