Furthermore, PilA of ssp. novicida was recently shown to be involved in protein secretion that was coupled to Tfp [20, 25]. Interestingly,

mutation of pilA and loss of protein secretion resulted in increased virulence in a mouse infection model [25]. As the human pathogenic type A and type B strains do not secrete detectable levels of proteins in vitro, it is possible that one step in the evolution of human pathogenic variants of F. tularensis from ssp. novicida has involved loss of protein secretion Decitabine manufacturer as a consequence of changes in PilA structure and function. In this work we wanted to address the question if PilA is involved in virulence of the highly pathogenic type A strain SCHU S4, similarly to

what we have previously shown for type B strains, and if Tfp secretion and assembly genes are required for virulence. Results Construction of non-polar pilin gene mutants In a recent study, we were able to demonstrate that the pilA gene can be lost by a deletion event mediated by direct repeats flanking the gene [22]. Type B strains lacking pilA were found to be attenuated for virulence in a mouse infection model. In this study we wanted to extend this work to the highly pathogenic type A strain SCHU S4, and therefore we constructed a specific pilA deletion mutant using our previously described allelic exchange technique [7]. In addition, to address the significance of secretion and Rapamycin assembly of PilA, we also engineered in-frame deletions in pilC and pilQ, encoding a transmembrane protein and a secretin, respectively. For some pathogens, Tfp expression is associated with a unique ability to retract the pili, a phenotype depending on the ATPase PilT. Interestingly, pilT appears to be functional in type A

strains, while it is a pseudogene in the less pathogenic type B strains. In order to elucidate if the expression of PilT could be correlated to the higher virulence of type A strains, we also constructed an in-frame deletion in the pilT 3-mercaptopyruvate sulfurtransferase gene. In order to verify that the mutations did not have a major impact on neighboring gene transcription, each region was analysed by RT-PCR on mRNA extracted from the mutant strains and compared to the isogenic wild-type strain (Fig. 1). Thereby we could confirm that none of the deletion events caused any polar effects on transcription. Both pilC and pilT are flanked by pseudogenes situated directly downstream of each gene that were found not to be transcribed neither in the wild-type nor in the pilC or pilT mutant strains. The upstream genes of pilC and pilT were readily transcribed at similar levels in the wild-type and mutant strains. In the case of the pilQ mutant, we could verify non-polarity on the downstream aroK gene. Figure 1 A-D. Analysis of gene transcription in wild-type and mutant strains of F. tularensis using RT-PCR of mRNA.

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058) and **(p < 0.05). Taylorellae do not obviously alter A. castellanii physiology In order to visualise the impact of taylorellae on A. castellanii physiology, we monitored the evolution of A. castellanii morphology over a 7-day incubation period in co-culture with T. equigenitalis, T. asinigenitalis, E. coli or Selleckchem Panobinostat L. pneumophila (Figure 4). When A. castellanii was cultivated with the amoeba-sensitive E. coli bacteria, we observed that the number of amoebae remained stable and that amoeba cells conserved their typical trophozoite appearance, although they became smaller over time probably as a result of the nutrient

limitation of the culture medium. In the presence of the amoeba-resistant L. pneumophila bacteria, we

observed a sharp drop in number of amoeba and a drastic change in the surviving A. castellanii cell morphology, which gradually shifted to a stress-induced cyst form. The results obtained for co-cultures with taylorellae were similar to those obtained buy Daporinad with E. coli, with the observation of a conserved trophozoite appearance, a relatively stable concentration of amoeba and a decrease in the size of amoebic cells. There was no evidence of amoebic cyst formation induced by the presence of T. equigenitalis or T. asinigenitalis. Figure 4 Evolution of A. castellanii monolayers following bacterial infections. Following infection with E. coli, T. equigenitalis, T. asinigenitalis or L. pneumophila, at an MOI of 50, A. castellanii monolayers were visualised http://www.selleck.co.jp/products/Staurosporine.html at an indicated time with an inverted microscope. To assess the toxicity of bacterial species to A. castellanii, amoebae were infected at an MOI of 50 with T. equigenitalis, T. asinigenitalis, E. coli or L. pneumophila. The viability of amoebic cells in infected monolayers was quantified at indicated time points by using Alamar blue dye (Figure 5). The cytotoxicity of L. pneumophila reached 80% after one week of incubation, whereas the cytotoxicity of T. equigenitalis, T. asinigenitalis and E. coli

to A. castellanii did not exceed 10% after one week. These data reveal that taylorellae have little cytotoxicity effects on A. castellanii. Figure 5 Taylorellae exhibit low cytotoxicity to A. castellanii . Acanthamoeba castellanii were infected with E. coli, T. equigenitalis, T. asinigenitalis or L. pneumophila with an MOI of 50. The viability of amoebic cells in infected monolayers was quantified at an indicated time using Alamar blue dye. These data are representative of two independent experiments done in triplicate. Each bar represents the mean of triplicate wells; error bars represent the standard deviations. Taylorellae are not able to grow on dead A. castellanii cells To determine the conditions which allowed taylorellae to persist in the presence of amoebae, we measured T. equigenitalis and T.

PubMedCrossRef 35. Kataoka M, Hashimoto K-I, Yoshida M, Nakamatsu T, Horinouchi S, Kawasaki FK506 in vitro H: Gene expression of Corynebacterium glutamicum in response to the conditions inducing glutamate overproduction. Lett Appl Microbiol 2006, 42:471–476.PubMedCrossRef 36. Lawrence AG, Schoenheit J, He A, Tian J, Liu P, Stubbe J, Sinskey AJ: Transcriptional analysis of Ralstonia eutropha genes related to poly-( R )-3-hydroxybutyrate homeostasis during batch fermentation. Appl Microbiol Biotechnol 2005, 68:663–672.PubMedCrossRef 37. Lindenkamp N, Peplinski K, Volodina E, Ehrenreich A, Steinbüchel A: Impact of multiple β-ketothiolase

deletion mutations in Ralstonia eutropha H16 on the composition of 3-mercaptopropionic acid-containing copolymers. Appl Environ Microbiol 2010, 76:5373–5382.PubMedCrossRef 38. Budde CF, Mahan AE, Lu J, Rha C, Sinskey AJ: Roles Depsipeptide in vivo of multiple acetoacetyl coenzyme A reductases in polyhydroxybutyrate biosynthesis in Ralstonia eutropha H16. J Bacteriol 2010, 192:5319–5328.PubMedCrossRef 39. Pötter M, Müller H, Steinbüchel A: Influence of homologous phasins (PhaP) on PHA accumulation and regulation of their expression by the transcriptional repressor PhaR in Ralstonia eutropha H16. Microbiology 2005, 151:825–833.PubMedCrossRef 40. Pötter M, Müller H, Reinecke F, Wieczorek R, Fricke F, Bowien B, Friedrich B, Steinbüchel A: The complex

structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha . Microbiology 2004, 150:2301–2311.PubMedCrossRef 41. Pfeiffer D, Jendrossek D: Interaction between poly(3-hydroxybutyrate) granule-associated proteins as revealed by two-hybrid analysis and identification of a new phasin in Ralstonia eutropha H16. Non-specific serine/threonine protein kinase Microbiology 2011, 157:2795–2807.PubMedCrossRef 42. Pfeiffer D, Jendrossek D: Localization of PHB granule associated

proteins during PHB granule formation and identification of two new phasins, PhaP6 and PhaP7, in Ralstonia eutropha H16. J Bacteriol 2012, 194:5909–5921.PubMedCrossRef 43. Pfeiffer D, Wahl A, Jendrossek D: Identification of a multifunctional protein, PhaM, that determines number, surface to volume ratio, subcellular localization and distribution to daughter cells of poly(3-hydroxybutyrate), PHB, granules in Ralstonia eutropha H16. Mol Microobiol 2011, 82:936–951.CrossRef 44. Kaddor C, Steinbüchel A: Effects of homologous phosphoenolpyruvate-carbohydrate phosphotransferase system proteins on carbohydrate uptake and poly(3-hydroxybutyrate) accumulation in Ralstonia eutropha H16. Appl Environ Microbiol 2011, 77:3582–3590.PubMedCrossRef 45. Michel H, Behr J, Harrenga A, Kannt A: Cytochrome c oxidase: structure and spectroscopy. Annu Rev Biophys Biomol Struct 1998, 27:329–356.PubMedCrossRef 46. Kato M, Bao HJ, Kang C-K, Fukui T, Doi Y: Production of a novel copolyester of 3-hydroxybutyric acid and medium-chain-length 3-hydroxyalkanoic acids by Pseudomonas sp. 61–3 from sugars. Appl Microbiol Biotechnol 1996, 45:363–370.CrossRef 47.

Vasc Cell 2011,3(1):20. doi:10.1186/2045-824X-3-20.PubMedCrossRef 27. Donnem T, Andersen S, Al-Shibli K, Al-Saad S, Busund LT, Bremnes RM: Prognostic impact of Notch ligands and receptors in non-small cell lung cancer: coexpression of Notch-1 and vascular endothelial growth factor-A predicts poor survival. Cancer 2010,

116:5676–5685.PubMedCrossRef Competing interests The authors declare that they have no competing interest. Authors’ contribution SI and AT wrote the manuscript. SN, YU and HO contributed conceptual information and edited the manuscript. All authors read and approved the final manuscript.”
“Introduction Lung cancer is the most common malignancy all over the world and the buy X-396 leading cause of death in men [1], and non-small cell lung cancer (NSCLC) accounts for >80% of primary lung cancers [2, 3]. Treatment of these patients is usually based on a multidisciplinary strategy, including a combination of radiotherapy and chemotherapy. However, results buy Nivolumab of these treatments were unsatisfactory with a 3-year overall survival (OS) being 10% to 20% [4]. The classic prognostic determinants for lung cancer include the tumor-node-metastasis staging system, performance status, sex, and weight loss. Unfortunately, all these

factors are far less than sufficient to explain the patient-to-patient variability. Therefore, identification of new biomarkers for more accurate prognostic and predictive assessment is warranted and could be helpful to highlight the possibility of patient-tailored decisions [5]. The skeleton is the most common site for distant metastasis in patients with cancer [6]. Tumor cells

homing to form bone metastases is common in non-small cell lung cancer (NSCLC), just like what is seen in breast, prostate and thyroid cancers [7, 8]. Some patients may experience bone metastasis many years after surgery of the primary tumor. The high morbidity and significantly increased risk of fractures associated with bone metastasis seriously affect patients’ quality Cediranib (AZD2171) of life. About 36% of all lung cancers and and 54.5% of stage II-IIIA NSCLC showed postoperative recurrence or metastasis [9]. Many lung cancer patients expect new and more sensitive markers to predict metastatic diseases. If bone metastasis can be predicted early enough, then effective prevention could be started and may result in an improvement in survival [10]. The molecular and cellular mechanisms leading to the development of bone metastasis in NSCLC remain unclear, so searching for effective biomarkers to predict the possibility of bone metastasis is valuable in clinical practice. OPN is a sibling glycoprotein that was first identified in 1986 in osteoblasts. OPN is a highly negatively charged, extracellular matrix protein that lacks an extensive secondary structure [11]. The OPN gene is composed of 7 exons, 6 of which contain coding sequence [12].

There were 9 cases which the co-expression of BCL-2 and BAD were negative, ER(+)PR(-)

was 1 case(11.1%), ER(-)PR(-) were 8 cases(88.9%), ER(+)PR(+) and ER(-)PR(+) click here were all 0;The negative co-expression rates of BCL-2 and BAD in the ER(-)PR(-) group were significantly higher than the other three groups (P < 0.05).(Table 4) Table 4 The relationship between the expression of BCL-2, BAD and the expression of ER, PR.   Total ER(+)PR(+) ER(+)PR(-) ER(-)PR(+) ER(-)PR(-) Bcl-2(+)Bad(+) 9 6(66.7%)a 2(22.2%)b 1(11.0%)c 0(0.0%)d Bcl-2(+)Bad(-) 40 18(45.0%) 10(25.0%) 7 (17.5%) 5 (12.5%) Bcl-2(-)Bad(+) 22 6(27.3%) 7(31.8%) 8(36.4%) 1(4.5%) Bcl-2(-)Bad(-) 9 0(0.0%) 1(11.1%)f 0(0.0%)g 8(88.9%)h a compared b.c.d P < 0.05; h comparede.f.g P < 0.05. 2.2.1 The Sensitivity Of Breast Cancer Cells To Anticancer Drugs In Vadimezan manufacturer Vitro The mean relative

inhibition rate of breast cancer cells are EADM(69.74 ± 7.67)%, 5-Fu(61.81 ± 9.94)%, NVB(69.10 ± 8.27)%, DDP(63.27 ± 6.79)% in 10 × PPC. The numerus are EADM(45.39 ± 11.74)%, 5-Fu(44.56 ± 12.28)%, NVB(48.50 ± 9.96)%, DDP(41.42 ± 4.81)% in 1 × PPC and EADM(27.57 ± 8.94)%, 5-Fu(25.48 ± 8.62)%, NVB(30.35 ± 9.02)%, DDP(25.33 ± 5.65)% in 0.1 × PPC. Along with drug concentrating reduction, breast cancer cancer cell’s inhibition rate relatively reduces gradually. The sensitivity of breast cancer cells to the 4 kinds of drugs in 0.1 × PPC are as follow EADM 30%, 5-Fu 20%, NVB 45%, DDP 25%(Table. 5). Table 5 Sensitivity rate of 20 breast cancer cells to 4 kinds anticancer drugs in 0.1 × PPC Drugs Desensitize(%) Sensitive(%) Midrange sensitive (%) Sensitivity rate(%) EADM 70 (14) 30 (6) 0 30 (6) 5-Fu 80 (16) 20 (4) 0 20 (4) NVB 55 (11) 35 (7) 10 (2) 45 (9) DDP 75 (15) 25 (5) 0 25 (5) 2.2.2 The Relationship Between The Expression Of BCL-2, BAD And The Chemosensitivity Of The Breast Cancer Cells In 0.1 × PPC In Vitro In the drug sensitivity test in vitro of breast cancer cells of 4 kinds of chemotherapeutic agents in 0.1 × PPC, the chemosensitivity and the expression level of

BCL-2 are related, the chemosensitivity of the Urease BCL-2(-) tumor cells was higher than the BCL-2(+) tumor cells(Table. 6), and there was a negative correlation between the the expression of BCL-2 and the chemosensitivity of the 4 drugs (P < 0.05). In the test the sensitivity to EADM and NVB were associated with the expression of BAD, The BAD(+)tumour cells were more sensitivity to EADM and NVB than the BAD(-)ones(P < 0.05)(Table. 7). and there was a positive correlation between the the expression of BAD and the chemosensitivity to EADM and NVB.

Key to the recognized species of Macrolepiota from China 1 Basidiomata with a volva at the base of the stipe M. velosa   1* Basidiomata without a volva at the base of the stipe 2 Pileus surface with brown

plate-like squamules; annulus complex; clamp connections common at the base of the basidia 3 Stipe surface with conspicuous fine brown squamules on whitish background; pileus squamules made up of yellowish-brown walled long hyphal segments, mainly 25–90 × 7–11 (14) μm M. procera   3* Stipe surface with fine brown squamules on whitish background; pileus squamules made up of yellowish-brown walled short hyphal segments, mainly 15–25 × 7–11 μm M. detersa     2* Pileus surface with pale ochraceous to brown fine squamules; annulus simple, or only slightly thicker near Lapatinib cell line the edge; clamp connections absent or present 4 Stipe surface with brown squamules; usually without clamps at the base of basidia M. mastoidea   4* Stipe surface smooth; usually with clamps at the base of basidia

5 Stipe base sometimes becomes orange when cut, pileus squamules composed of more frequently branched hyphae, cheilocystidia mainly clavate to broadly clavate M. dolichaula   5* Stipe base not changing color when cut, pileus squamules composed of seldom branched hyphae, cheilocystidia mainly obtusely fusiform to clavate M. orientiexcoriata         Discussion New species within Macrolepiota and species diversity in China As shown in Fig. 1, M. detersa is phylogenetically closely related to, but distinct from M. dolichaula and M. procera Gefitinib concentration based on the ITS data. Similarly,

M. orientiexcoriata is phylogenetically closely related to M. excoriata, M. mastoidea, and M. phaeodisca, but forms a clade of its own. As both M. detersa and M. orientiexcoriata have discrete characters to tell them apart from the currently described species, we described them as new species in this paper. In addition, the result that M. detersa clustered with 3 collections of M. sp. from Japan, which as a whole gets strong statistical supports, 100% of bootstrap and 1.00 bayesian PP support respectively, indicates that the three Urease Japanese collections are M. detersa (Fig. 1). By far, Europe is the species richest region of Macrolepiota, with 11 species in the current sense recorded (Candusso and Lanzoni 1990; Vellinga 2001; but numbers depend on species concepts), then followed by Asia with 9 species recorded (Manjula 1983; Pegler 1986; Shao and Xiang 1981; Teng 1996; Vellinga and Yang 2003), and 4 species in east Africa (Pegler 1977), and 3 species in Australia (Grgurinovic 1997; Vellinga 2003). Based on our present results, at least 6 morphological species were found in China, with representatives belonging to three different phylogenetic clades recovered by the analyses of the ITS data set.

L. plantarum (4/19 and 12/15 for T-CD and HC, respectively), L. casei (5/19 and 5/15 for T-CD and HDAC inhibitor HC, respectively) and L. rhamnosus (2/19 and 2/15 for

T-CD and HC, respectively) were the species of lactobacilli which were most largely isolated in both T-CD and HC. On the contrary, Lactobacillus salivarius (4/19), Lactobacillus coryneformis (2/19), Lactobacillus delbrueckii subsp. bulgaricus (1/19), Lactobacillus fermentum (1/19) and L. paracasei (1/19) were only identified in faecal samples of T-CD. Lactobacillus brevis (1/15), Lactobacillus pentosus (1/15) and Lactobacillus mucosae (1/15) were only identified in faecal samples of HC. Table 2 Species of the Lactobacillus and Enterococcus genera identified in faecal samples by 16S rRNA and pheS or recA gene sequencing Sample Number of isolates Number of strains identifieda Closest relative and identity (%) Accession Number Treated celiac disease (T-CD) children 1 3 3-IVb Pediococcus pentosaceus (99%) [GenBank:FJ844959.1]   1, 7 1-VII, 5-XI Enterococcus faecium (99%) [GenBank:FJ982664.1]   1 1-XII Enterococcus avium (99%) [GenBank:HQ169120.1]   1 1-20I Lactobacillus plantarum (99%) [GenBank:HQ441200.1]   1 1-7I ICG-001 cell line Lactobacillus delbrueckii subsp. bulgaricus (99%) [GenBank:CP002341.1]

2 12 6-IV Pediococcus pentosaceus (99%) [GenBank:FJ844959.1] 3 2, 1, 1 2-XIV, 1-6I, 1-1I Enterococcus faecium (99%) [GenBank:HQ293070.1]   6 6-XVI Enterococcus faecalis (99%) [GenBank:HQ293064.1]   1 1-9I Lactobacillus salivarius (99%) [GenBank:GU357500.1] 4 1, 3, 2 1-II, 3-V, 2-VII Enterococcus faecium (99%) [GenBank:HQ293070.1]   3, 1, 1 3-II, 1-IV, 1-V Enterococcus avium (99%) [GenBank:HQ169120.1]

  1 1-24I Lactobacillus casei (99%) [GenBank:HQ379174.1] Docetaxel purchase   1 1-11I Lactobacillus plantarum (99%) [GenBank:EF439680.1] 5 5 5-VII Enterococcus faecium (99%) [GenBank:FJ982664.1]   1, 3 1-6I, 2-XIX Enterococcus sp. (99%) [GenBank:AB470317.1]   1 1-11I Lactobacillus rhamnosus (99%) [GenBank:HM218396.1]   1, 1 1-1I, 1-8I Lactobacillus fermentum (99%) [GenBank:HQ379178.1] 6 5 1(5I-11I-7I-12I-2I) Enterococcus avium (99%) [GenBank:HQ169120.1]   4 3-XXII Enterococcus sp. (99%) [GenBank:AB470317.1]   1, 1 1-1I, 1-3I Lactobacillus plantarum (99%) [GenBank:EF439680.1] 7 1 1-12I Enterococcus avium (99%) [GenBank:HQ169120.1]   11 4-XX Streptococcus macedonicus (99%) [GenBank:EU163501.1] 8 1 1-VII Enterococcus faecium (99%) [GenBank:HQ293070.1]   1 1-14I Enterococcus sp. (99%) [GenBank:AB470317.1]   4, 3, 1, 1, 1, 1 4-III, 3-IV, 1-6I, 1-12I, 1-14I, 1-15I Lactobacillus salivarius (99%) [GenBank:FJ378897.1] 9 2, 3 1-III,3-IV Enterococcus faecalis (99%) [GenBank:HQ293064.1]   1, 1, 1, 3, 1 10I, 1-V, 1-VI, 3-VII, 1-2I Enterococcus faecium (99%) [GenBank:HQ293070.1] Treated celiac disease (T-CD) children   1 1-14Ib Lactobacillus casei (99%) [GenBank:HQ318715.2] 10 1 1-III Enterococcus faecalis (99%) [GenBank:HQ293064.1]   1 1-VII Enterococcus durans (99%) [GenBank:HM218637.

Mol Microbiol 2005, 55:1883–1895.PubMedCrossRef 65. Christner M, Franke G, Schommer N, Wendt U, Wegert K, Pehle P, Kroll G, Schulze C, Buck F, Mack

D, Aepfelbacher M, Rohde H: The giant extracellular matrix binding protein of Staphylococcus epidermidis mediates biofilm accumulation and attachment to fibronectin. Mol Microbiol 2010, 75:187–207.PubMedCrossRef 66. Arciola CR, Baldassarri L, Montanaro : Presence of icaA and icaD Genes and Slime Production in a Collection of Staphylococcal Strains from Catheter-Associated Infections. J Clin Microbiol 2001, 39:2151–2156.PubMedCrossRef 67. De Silva GDI, Kantzanou M, Justice A, Massey RC, Wilkinson AR, Day NPJ, Peacock SJ: The ica operon and biofilm production in coagulase-negative staphylococci associated with carriage and disease in a neonatal intensive care unit. J Clin Akt inhibitor Microbiol

2002, 40:382–388.PubMedCrossRef 68. Ziebuhr W, Krimmer V, Rachid S, Lobner I, Gotz F, Hacker J: A novel mechanism of phase variation of virulence in Staphylococcus epidermidis: evidence for control of the polysaccharide intercellular adhesin synthesis by alternating insertion and excision of the insertion sequence element IS256. Mol Microbiol 1999, 32:345–350.PubMedCrossRef 69. Nilsdotter-Augustinsson A, Koskela A, Öhman L, Söderquist B: Characterization of coagulase-negative Panobinostat in vitro staphylococci isolated from patients with infected hip prostheses: use of phenotypic and genotypic analyses, including tests for the presence of the ica operon. Eur J Clin Microbiol Infect Dis 2007, 26:255–265.PubMedCrossRef 70. Mack D, Bartscht K, Fischer C, Rohde H, De Grahl C, Dobinsky

S, Horstkotte MA, Kiel K, Knobloch JK-M: Genetic and Biochemical Analysis of Staphylococcus epidermidis Biofilm Accumulation. Meth Enzymol 2001, 336:215–239.PubMedCrossRef Authors’ contributions AS carried out experimental work and drafted the manuscript. FK designed and participated in experiments involving analysis of clinical strains. MK participated in experiments for 20-kDaPS isolation and helped to draft the manuscript. LH participated in experiments involving comparison of PIA and 20-kDaPS by immunofluorescence PAK5 and contributed to design of these experiments. TW participated in experiments involving comparison of PIA and 20-kDaPS by ELISA and contributed to design of these experiments. AD participated in the design of the study. GD contributed to design of phagocytosis experiments. NK contributed to design of phagocytosis experiments, structural elucidation, data interpretation and revised the manuscript. DM designed the study and experimental work involving comparison of PIA and 20-kDaPS, interpreted acquired data and revised the manuscript.

MinD, a membrane-bound ATPase, recruits MinC to inhibit FtsZ polymerization at the non-division ABT 888 site [4, 5]. MinE forms a dynamic ring that undergoes a repetitive cycle of movement first to one pole and then to the opposite pole in the cell [6], and induces conformational

changes in membrane-bound MinD [7], which results in release of MinC and conversion of membrane-bound MinD (MinD:ATP) to cytoplasmic MinD (MinD:ADP) [7]. This highly dynamic localization cycle of Min proteins inhibits FtsZ ring formation near cell ends and forces FtsZ and many other cell division proteins to assembly at the center of the cell [8]. FtsZ and Min proteins are conserved in a wide variety of bacteria, including cyanobacteria [9]. As endosymbionts in plant cells, chloroplasts have inherited many characters from their ancestor, cyanobacteria [10]. For example, FtsZ, MinD, MinE and ARC6 are chloroplast division proteins evolved from cyanobacteria cell division proteins [9]. Besides the similarity shared with their ancestors, some new characters were gained in these proteins during evolution. The FtsZ family in Arabidopsis includes AtFtsZ1, which lacks the conserved Peptide 17 price C-terminal domain [11]; AtFtsZ2-1 and AtFtsZ2-2 [12], which are more similar to the FtsZ in cyanobacteria than other members [13]; and ARC3, which has a much less conserved GTPase domain of FtsZ and a later acquired C-terminal MORN repeat

domain [14]. All these FtsZ homologues can form a ring at the chloroplast division site [15, Fossariinae 16]. Similar to their homologues in bacteria, MinD and MinE in Arabidopsis have been shown to be involved in the positioning of the division site in chloroplasts [17–19]. Antisense suppression of AtMinD or a single mutation in AtMinD cause misplacement of the chloroplast division site in Arabidopsis [17, 20]. AtMinE antagonizes the function of AtMinD [19]. Overexpression of AtMinE

in Arabidopsis results in a phenotype similar to that caused by antisense suppression of AtMinD [19]. However, AtMinD has been shown to be localized to puncta in chloroplasts [20] and never been reported to oscillate. This is quite different from that of EcMinD in E. coli. To study the function of AtMinD, we expressed it in E. coli HL1 mutant which has a deletion of EcMinD and EcMinE and a minicell phenotype [21]. Surprisingly, the mutant phenotype was complemented. Similar to the localization in chloroplasts [20], AtMinD was localized to puncta at the poles in E. coli HL1 mutant without oscillation in the absence of EcMinE. We also confirmed that AtMinD can interact with EcMinC. AtMinD may function through EcMinC by prevent FtsZ polymerization at the polar regions of the cell. Our data suggest that the cell division of E. coli can occur at the midcell with a non-oscillating Min system which includes AtMinD and EcMinC and the working mechanism of AtMinD in chloroplasts may be different from that of EcMinD in E.