1991
DOI: 10.1016/0378-1097(91)90009-y
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Sequence analysis of the Legionella micdadei groELS operon

Abstract: A 2.7 kb DNA fragment encoding the 60 kDa common antigen (CA) and a 13 kDa protein of Legionella micdadei was sequenced. Two open reading frames of 57,677 and 10,456 Da were identified, corresponding to the heat shock proteins GroEL and GroES, respectively. Typical -35, -10, and Shine-Dalgarno heat shock expression signals were identified upstream of the L. micdadei groEL gene. Further upstream, a poly-T region, also a feature of the sigma 32-regulated Escherichia coli groELS heat shock operon, was found. Desp… Show more

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Cited by 9 publications
(7 citation statements)
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References 12 publications
(16 reference statements)
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“…The amino acid sequence deduced from the nucleotide sequence agreed completely with those suggested by the Edman degradation for oligopeptides from symbionin (Kakeda and Ishikawa, unpublished). Molecular weight deduced for the gene product was also consistent with moDiscussion So far, over 15 genes for bacterial and organellar cpn60 have been sequenced to permit comparison among deduced amino acid sequences of these proteins (Gupta 1990;Peralta et al 1990;Martel et al 1990;Chitnis and Nelson 1991;Hindersson et al 1991;Shanafelt et al 1991;Miller et al 1991). It has been shown, for example, that yeast hsp60 (Reading et al 1989), ribulose bisphosphate carboxylase/ oxygenase subunit binding protein (Hemmingsen et al 1988), 62-kDa antigen from Coxiella burnetii (Vodkin and Williams 1988), and 65-kDa antigen from Mycobacterium leprae (Mehra et al 1986) are 53%, 49%, 75%, and 59% identical to the E. coli GroEL protein, respectively (Gupta 1990).…”
Section: Resultssupporting
confidence: 56%
“…The amino acid sequence deduced from the nucleotide sequence agreed completely with those suggested by the Edman degradation for oligopeptides from symbionin (Kakeda and Ishikawa, unpublished). Molecular weight deduced for the gene product was also consistent with moDiscussion So far, over 15 genes for bacterial and organellar cpn60 have been sequenced to permit comparison among deduced amino acid sequences of these proteins (Gupta 1990;Peralta et al 1990;Martel et al 1990;Chitnis and Nelson 1991;Hindersson et al 1991;Shanafelt et al 1991;Miller et al 1991). It has been shown, for example, that yeast hsp60 (Reading et al 1989), ribulose bisphosphate carboxylase/ oxygenase subunit binding protein (Hemmingsen et al 1988), 62-kDa antigen from Coxiella burnetii (Vodkin and Williams 1988), and 65-kDa antigen from Mycobacterium leprae (Mehra et al 1986) are 53%, 49%, 75%, and 59% identical to the E. coli GroEL protein, respectively (Gupta 1990).…”
Section: Resultssupporting
confidence: 56%
“…The values for the GroEL proteins are given above the 100% diagonal, and those for the GroES proteins below this diagonal. GroES was from B. subtilis C. acetobutylicum (24), M. tuberculosis (2), S. albus 58 (20), E. coli (16), C. trachomatis (23), C. bumetu (39), L. micdadei (17), and Synechocystis sp. strain PCC 6803 (7).…”
Section: Materuils and Methodsmentioning
confidence: 99%
“…strain PCC 6803 (7). GroEL was from B. subtilis, C. acetobutylicum (24), M. tuberculosis (33), S. albus (20), E. coli (16), C. trachomatis (23), C. bumetii (39), L. micdadei (17), and Synechococcus sp. strain PCC 7942 (35).…”
Section: Materuils and Methodsmentioning
confidence: 99%
“…We determined the complete nucleotide (nt) sequence of the groEx operon of X-bacteria and found the nt sequence of groEL,x to have a high degree of identity with those of other bacterial groEL genes, especially those living inside other cells, such as Legionella [46,481 and Coxiella [128]. A dendrogram constructed on the basis of amino acid sequences of GroEL analogs using the PAUP program, placed X-bacteria very close to L. pneumophila and C. burnetii.…”
Section: Micrurgical Manipulations In Amoebaementioning
confidence: 99%