Microtubular structures in a stable staphylococcal L-form

Eda, Tohru; Kanda, Yuko; Mori, Chizuru; Kimura, Sadao

doi:10.1128/jb.132.3.1024-1026.1977

Cited by 16 publications

(3 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although in prokaryotic cells a cytoskeleton has not been described so far, different researchers have reported the presence of several structures and proteins associated with this organelle (Eda, 1977; Nakamura & Watanabe, 1978; Nakamura et al ., 1978; Góbel et al ., 1981; Sioud et al ., 1987; Hiraga, 1993; Lutkenhaus, 1993; Korolev et al ., 1994). Functions proposed for prokaryotic actin-like proteins have included motility in the absence of locomotor appendages and maintenance of cell shape without a cell wall in Mycoplasma pneumoniae (Neimark, 1977).…”

Section: Introductionmentioning

confidence: 99%

Actin-related proteins in Anabaena spp. and Escherichia coli

et al. 1996

View full text Add to dashboard Cite

Actin has been described in all eukaryotic cells as the major microfilament cytoskeletal protein. Although prokaryotic cells do not have a cytoskeleton, proteins related to the latter have been found in different prokaryotic species. We have found prokaryotic actin-related proteins in the enterobacterium Escherichia coli and in the cyanobacteria Anabaena cylindrica and Anabaena variabilis. They were identified by the following criteria: (1) by cross-reaction with a fluorescent conjugated anti-actin (rat-brain) mAb by Western blot analysis (in total cellular extracts); (2) specific binding of acetone powder and soluble cellular extracts to DNase 1; and (3) specific binding of cells and total cellular extracts to phalloidin. In E. coli, specific binding of phalloidin labelled with rhodamine to cells was detected by spectrofluorometry. In total cellular extracts, three bands of 60, 43 and 35 kDa were weakly recognized by the mAb by Western blot analysis; this recognition increased when phalloidin was added to the extracts. Furthermore, three polypeptides of 60 kDa were isolated by binding to DNase I, showing pl values of 6.7, 6.65 and 6.6, less acidic than all reported actin pl values. In A. cylindrica and A. variabilis, specific binding of phalloidin labelled with rhodamine to cells was also detected by spectrofluorometry. In total and soluble cellular extracts, the mAb recognized two bands of 45 and 40 kDa by Western blot analysis, but only the first was purified by binding to DNase I, and it showed three isoforms of pl values 6.8, 6.5 and 6.4. These results suggest the presence, in prokaryotes, of proteins with similar biochemical characteristics to eukaryotic actin.

show abstract

Section: Introductionmentioning

confidence: 99%

Actin-related proteins in Anabaena spp. and Escherichia coli

et al. 1996

View full text Add to dashboard Cite

show abstract

“…Bar, 500 nm (in panel A) and 100 nm (in panels B and C). have been associated with altered protein synthesis (6,8,11). Small ellipsoid particles (10) and small dense particles (14), both types found in P. mirabilis, were interpreted as products of defective phage synthesis and were thus called phage-like particles, whereas typical phages have so far not been found.…”

Section: Fig 3 Panel Amentioning

confidence: 99%

“…Tubular and other regular structures have been described in earlier electron microscopic studies of the L forms of various species of bacteria (6,8,9,11). Although some of these structures, occuring in the L form of Proteus mirabilis, were described as resembling incomplete phages (phage-like structures) (10,14), there has until now been no evidence for complete phages in thin-sectioned L-form colonies.…”

mentioning

confidence: 97%

Bacteriophages in L form of Staphylococcus aureus

Schmid¹

1985

J Bacteriol

View full text Add to dashboard Cite

show abstract

Ultrastructural characterization of core structures and paracrystalline inclusion bodies in L‐form cells of streptomycetes

Gumpert

1983

J of Basic Microbiology

View full text Add to dashboard Cite

Protoplast type L‐form cells of Streptomyces hygroscopicus and S. griseus contain different types of inclusion bodies. Cytoplasmic cores and paracrystalline structures are peculiar inclusions which could not be observed in normal parent bacteria. The cytoplasmic cores are 1–4 μm long and 0.05–0.25 μm broad straight and stiff non‐tubular structures consisting of homogeneous moderate electron opaque material. Paracrystalline inclusions have side‐lengths between 0.2 and 0.5 μm and show a characteristic pattern of 15–20 nm thick straight dark lines and electron lucent intervening spaces of 20–30 nm. Both cytoplasmic cores and paracrystalline inclusions are apparently proteins. Their occurrence in L‐form cells indicates an altered synthesis of one or several proteins in these cell types.

show abstract

Microtubular structures in a stable staphylococcal L-form

Abstract: Microtubular structures, which were demonstrated as straight, dense-walled cylinders attached to cell membranes, were found in a stable staphylococcal Lform grown in the absence of antibiotic.

Cited by 16 publications

References 4 publications

Actin-related proteins in Anabaena spp. and Escherichia coli

Actin-related proteins in Anabaena spp. and Escherichia coli

Bacteriophages in L form of Staphylococcus aureus

Ultrastructural characterization of core structures and paracrystalline inclusion bodies in L‐form cells of streptomycetes

Contact Info

Product

Resources

About