Taxonomic analysis of Sorangium strains based on HSP60 and 16S rRNA gene sequences and morphology

Jiang, Deming; Zhao, Lin; Zhang, Cuiying; Li, Jian; Xia, Zhi‐Jie; Wang, Jing; Wu, Zhihong; Li, Yuezhong

doi:10.1099/ijs.0.65806-0

Cited by 14 publications

(6 citation statements)

References 14 publications

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“…Myxobacteria encode two groEL paralogs: groEL1 and groEL2, which are 83 and 79 % identical at the gene and protein levels, respectively (Jiang et al 2008). While groEL1 exists in the conventional bicistronic operon with an upstream groES gene, groEL2 exists separately (Li et al 2010).…”

Section: Multiple Groels In Myxobacteria-living In Relationmentioning

confidence: 99%

Multiple chaperonins in bacteria—novel functions and non-canonical behaviors

Kumar

Mande

Mahajan

2015

Cell Stress and Chaperones

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Chaperonins are a class of molecular chaperones that assemble into a large double ring architecture with each ring constituting seven to nine subunits and enclosing a cavity for substrate encapsulation. The well-studied Escherichia coli chaperonin GroEL binds non-native substrates and encapsulates them in the cavity thereby sequestering the substrates from unfavorable conditions and allowing the substrates to fold. Using this mechanism, GroEL assists folding of about 10-15 % of cellular proteins. Surprisingly, about 30 % of the bacteria express multiple chaperonin genes. The presence of multiple chaperonins raises questions on whether they increase general chaperoning ability in the cell or have developed specific novel cellular roles. Although the latter view is widely supported, evidence for the former is beginning to appear. Some of these chaperonins can functionally replace GroEL in E. coli and are generally indispensable, while others are ineffective and likewise are dispensable. Additionally, moonlighting functions for several chaperonins have been demonstrated, indicating a functional diversity among the chaperonins. Furthermore, proteomic studies have identified diverse substrate pools for multiple chaperonins. We review the current perception on multiple chaperonins and their physiological and functional specificities.

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Section: Multiple Groels In Myxobacteria-living In Relationmentioning

confidence: 99%

Multiple chaperonins in bacteria—novel functions and non-canonical behaviors

Kumar

Mande

Mahajan

2015

Cell Stress and Chaperones

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“…A final example of the role of multiple Cpn60 proteins in the lifestyle of prokaryotes is the two Cpn60 proteins of the Gram-negative myxobacterium, Myxococcus xanthus (Jiang et al, 2008). The myxobacteria have a complex social behaviour, forming gliding colonies called swarms that can feed on other microorganisms.…”

Section: Chaperonin 60: An Evolutionarily Diverse Molecular Chapementioning

confidence: 99%

Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions

2013

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Chaperonin 60 is the prototypic molecular chaperone, an essential protein in eukaryotes and prokaryotes, whose sequence conservation provides an excellent basis for phylogenetic analysis. Escherichia coli chaperonin 60 (GroEL), the prototype of this family of proteins, has an established oligomeric-structure-based folding mechanism and a defined population of folding partners. However, there is a growing number of examples of chaperonin 60 proteins whose crystal structures and oligomeric composition are at variance with GroEL, suggesting that additional complexities in the protein-folding function of this protein should be expected. In addition, many organisms have multiple chaperonin 60 proteins, some of which have lost their protein-folding ability. It is emerging that this highly conserved protein has evolved a bewildering variety of additional biological functions - known as moonlighting functions - both within the cell and in the extracellular milieu. Indeed, in some organisms, it is these moonlighting functions that have been left after the loss of the protein-folding activity. This highlights the major paradox in the biology of chaperonin 60. This article reviews the relationship between the folding and non-folding (moonlighting) activities of the chaperonin 60 family and discusses current knowledge on their molecular evolution focusing on protein domains involved in the non-folding chaperonin functions in an attempt to understand the emerging biology of this evolutionarily ancient protein family.

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“…The strain was morphologically and phylogenetically classified using previously reported methods Jiang et al, 2008). The genomic DNA of Sorangium cellulosum strain So0157-2 was extracted by a Genome Extract kit (Tiangen, China).…”

Section: Microorganism and Culture Conditionsmentioning

confidence: 99%

Glycosylation and production characteristics of epothilones in alkali-tolerant Sorangium cellulosum strain So0157-2

Zhao

Chen

et al. 2010

J Microbiol.

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3-O-alpha-D-ribofuranosyl epothilone A (epothiloneoside A) is a major component of glycosylated epothilones in Sorangium cellulosum strain So0157-2. The production and glycosylation ratios of epothiloneoside A in both solid and liquid culture conditions with various pH values and carbon sources were studied. The results showed that glycosylation occurs whenever epothilones are produced, regardless of changes in pH values, production time curves, and different carbon sources. We suggest that glycosylation is a stable process, paralleling the biosynthesis of epothilones in the So0157-2 strain.

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Taxonomic analysis of Sorangium strains based on HSP60 and 16S rRNA gene sequences and morphology

Cited by 14 publications

References 14 publications

Multiple chaperonins in bacteria—novel functions and non-canonical behaviors

Multiple chaperonins in bacteria—novel functions and non-canonical behaviors

Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions

Glycosylation and production characteristics of epothilones in alkali-tolerant Sorangium cellulosum strain So0157-2

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