scholarly journals SMC Protein-Dependent Chromosome Condensation during Aerial Hyphal Development in Streptomyces

2008 ◽  
Vol 191 (1) ◽  
pp. 310-319 ◽  
Author(s):  
Agnieszka Kois ◽  
Magdalena Świątek ◽  
Dagmara Jakimowicz ◽  
Jolanta Zakrzewska-Czerwińska
Keyword(s):  
Chromosome Segregation ◽  
Joint Action ◽  
Streptomyces Coelicolor ◽  
Chromosome Condensation ◽  
Higher Order ◽  
Binary Fission ◽  
Vegetative Mycelium ◽  
Chromosome Dynamics ◽  
Aerial Hyphae ◽  
Smc Proteins

ABSTRACT Members of the SMC (structural maintenance of chromosomes) protein family play a central role in higher-order chromosome dynamics from bacteria to humans. So far, studies of bacterial SMC proteins have focused only on unicellular rod-shaped organisms that divide by binary fission. The conversion of multigenomic aerial hyphae of the mycelial organism Streptomyces coelicolor into chains of unigenomic spores requires the synchronous segregation of multiple chromosomes. Here we focus on the contribution of SMC proteins to sporulation-associated chromosome segregation in S. coelicolor. Deletion of the smc gene causes aberrant DNA condensation and missegregation of chromosomes (7.5% anucleate spores). In vegetative mycelium, immunostained SMC proteins were observed sporadically, while in aerial hyphae about to undergo sporulation they appeared as irregularly spaced foci which accompanied but did not colocalize with ParB complexes. Our data demonstrate that efficient chromosome segregation requires the joint action of SMC and ParB proteins. SMC proteins, similarly to ParAB and FtsZ, presumably belong to a larger group of proteins whose expression is highly induced in response to the requirement of aerial hyphal maturation.

scholarly journals Dynamic interplay of ParA with the polarity protein, Scy, coordinates the growth with chromosome segregation in Streptomyces coelicolor

Open Biology ◽  
2013 ◽  
Vol 3 (3) ◽  
pp. 130006 ◽  
Author(s):  
Bartosz Ditkowski ◽  
Neil Holmes ◽  
Joanna Rydzak ◽  
Magdalena Donczew ◽  
Martyna Bezulska ◽  
...  
Keyword(s):  
Cell Division ◽  
Chromosome Segregation ◽  
Tip Growth ◽  
Streptomyces Coelicolor ◽  
Proximal Region ◽  
Cytoskeletal Protein ◽  
Mutant Form ◽  
Bacterial Cell Division ◽  
Aerial Hyphae ◽  
Dynamic Interplay

Prior to bacterial cell division, the ATP-dependent polymerization of the cytoskeletal protein, ParA, positions the newly replicated origin-proximal region of the chromosome by interacting with ParB complexes assembled on parS sites located close to the origin. During the formation of unigenomic spores from multi-genomic aerial hyphae compartments of Streptomyces coelicolor , ParA is developmentally triggered to form filaments along the hyphae; this promotes the accurate and synchronized segregation of tens of chromosomes into prespore compartments. Here, we show that in addition to being a segregation protein, ParA also interacts with the polarity protein, Scy, which is a component of the tip-organizing centre that controls tip growth. Scy recruits ParA to the hyphal tips and regulates ParA polymerization. These results are supported by the phenotype of a strain with a mutant form of ParA that uncouples ParA polymerization from Scy. We suggest that the ParA–Scy interaction coordinates the transition from hyphal elongation to sporulation.

scholarly journals Structural and Genetic Analysis of the BldB Protein of Streptomyces coelicolor

2002 ◽  
Vol 184 (15) ◽  
pp. 4270-4276 ◽  
Author(s):  
Marcus Eccleston ◽  
Reem Ahmed Ali ◽  
Richard Seyler ◽  
Janet Westpheling ◽  
Justin Nodwell
Keyword(s):  
Amino Acid ◽  
Genetic Analysis ◽  
Streptomyces Coelicolor ◽  
Higher Order ◽  
Order Complex ◽  
Amino Acid Residues ◽  
Dimer Formation ◽  
Aerial Hyphae

ABSTRACT We have demonstrated that the bldB gene of Streptomyces coelicolor is required for the formation of aerial hyphae and the synthesis of antibiotics. We also found that BldB forms a higher-order complex (most likely a dimer) and that amino acid residues 20 to 78 are important for this interaction. This region is conserved in the BldB family, suggesting that dimer formation may be a common feature of these proteins.

scholarly journals Replisome Localization in Vegetative and Aerial Hyphae of Streptomyces coelicolor

2006 ◽  
Vol 188 (20) ◽  
pp. 7311-7316 ◽  
Author(s):  
Beata Ruban-Ośmiałowska ◽  
Dagmara Jakimowicz ◽  
Aleksandra Smulczyk-Krawczyszyn ◽  
Keith F. Chater ◽  
Jolanta Zakrzewska-Czerwińska
Keyword(s):  
Green Fluorescent Protein ◽  
Enhanced Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Streptomyces Coelicolor ◽  
Aerial Mycelium ◽  
Vegetative Mycelium ◽  
Single Compartment ◽  
Aerial Hyphae ◽  
Green Fluorescent ◽  
Replication Activity

ABSTRACT Using a functional fusion of DnaN to enhanced green fluorescent protein, we examined the subcellular localization of the replisome machinery in the vegetative mycelium and aerial mycelium of the multinucleoid organism Streptomyces coelicolor. Chromosome replication took place in many compartments of both types of hypha, with the apical compartments of the aerial mycelium exhibiting the highest replication activity. Within a single compartment, the number of “current” ongoing DNA replications was lower than the expected chromosome number, and the appearance of fluorescent foci was often heterogeneous, indicating that this process is asynchronous within compartments and that only selected chromosomes undergo replication.

scholarly journals Dimerization of the RamC Morphogenetic Protein of Streptomyces coelicolor

2004 ◽  
Vol 186 (5) ◽  
pp. 1330-1336 ◽  
Author(s):  
Michael E. Hudson ◽  
Justin R. Nodwell
Keyword(s):  
Protein Kinase ◽  
Streptomyces Coelicolor ◽  
Kinase Domain ◽  
Terminal Protein ◽  
Amino Terminal ◽  
Morphogenetic Protein ◽  
Aerial Hyphae ◽  
Multiple Copies ◽  
Defective Allele

ABSTRACT RamC is required for the formation of spore-forming cells called aerial hyphae by the bacterium Streptomyces coelicolor. This protein is membrane associated and has an amino-terminal protein kinase-like domain, but little is known about its mechanism of action. In this study we found that the presence of multiple copies of a defective allele of ramC inhibits morphogenesis in S. coelicolor, consistent with either titration of a target or formation of inactive RamC multimers. We identified a domain in RamC that is C terminal to the putative kinase domain and forms a dimer with a Kd of ∼0.1 μM. These data suggest that RamC acts as a dimer in vivo.

scholarly journals Developmental-Stage-Specific Assembly of ParB Complexes in Streptomyces coelicolor Hyphae

2005 ◽  
Vol 187 (10) ◽  
pp. 3572-3580 ◽  
Author(s):  
Dagmara Jakimowicz ◽  
Bertolt Gust ◽  
Jolanta Zakrzewska-Czerwinska ◽  
Keith F. Chater
Keyword(s):  
Green Fluorescent Protein ◽  
Developmental Stage ◽  
Enhanced Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Streptomyces Coelicolor ◽  
Green Fluorescent Protein Fusion ◽  
Protein Fusion ◽  
Chromosome Partitioning ◽  
Aerial Hyphae ◽  
Green Fluorescent

ABSTRACT In Streptomyces coelicolor ParB is required for accurate chromosome partitioning during sporulation. Using a functional ParB-enhanced green fluorescent protein fusion, we observed bright tip-associated foci and other weaker, irregular foci in S. coelicolor vegetative hyphae. In contrast, in aerial hyphae regularly spaced bright foci accompanied sporulation-associated chromosome condensation and septation.

scholarly journals The Product of a Developmental Gene, crgA, That Coordinates Reproductive Growth in Streptomyces Belongs to a Novel Family of Small Actinomycete-Specific Proteins

2003 ◽  
Vol 185 (22) ◽  
pp. 6678-6685 ◽  
Author(s):  
Ricardo Del Sol ◽  
Andrew Pitman ◽  
Paul Herron ◽  
Paul Dyson
Keyword(s):  
Antibiotic Production ◽  
Streptomyces Coelicolor ◽  
Orthologous Gene ◽  
Streptomyces Avermitilis ◽  
Antibiotic Biosynthesis ◽  
Reproductive Growth ◽  
Solid Media ◽  
Aerial Hyphae ◽  
A Chain ◽  
Membrane Spanning

ABSTRACT On solid media, the reproductive growth of Streptomyces involves antibiotic biosynthesis coincident with the erection of filamentous aerial hyphae. Following cessation of growth of an aerial hypha, multiple septation occurs at the tip to form a chain of unigenomic spores. A gene, crgA, that coordinates several aspects of this reproductive growth is described. The gene product is representative of a well-conserved family of small actinomycete proteins with two C-terminal hydrophobic-potential membrane-spanning segments. In Streptomyces avermitilis, crgA is required for sporulation, and inactivation of the gene abolished most sporulation septation in aerial hyphae. Disruption of the orthologous gene in Streptomyces coelicolor indicates that whereas CrgA is not essential for sporulation in this species, during growth on glucose-containing media, it influences the timing of the onset of reproductive growth, with precocious erection of aerial hyphae and antibiotic production by the mutant. Moreover, CrgA subsequently acts to inhibit sporulation septation prior to growth arrest of aerial hyphae. Overexpression of CrgA in S. coelicolor, uncoupling any nutritional and growth phase-dependent regulation, results in growth of nonseptated aerial hyphae on all media tested, consistent with a role for the protein in inhibiting sporulation septation.

scholarly journals AdpA, key regulator for morphological differentiation regulates bacterial chromosome replication

Open Biology ◽  
2012 ◽  
Vol 2 (7) ◽  
pp. 120097 ◽  
Author(s):  
Marcin Wolański ◽  
Dagmara Jakimowicz ◽  
Jolanta Zakrzewska-Czerwińska
Keyword(s):  
Streptomyces Coelicolor ◽  
Morphological Differentiation ◽  
Chromosome Replication ◽  
Dependent Manner ◽  
Atp Levels ◽  
Aerial Hyphae ◽  
Preferential Binding ◽  
Transcription Regulators ◽  
Initiation Stage

AdpA, one of the most pleiotropic transcription regulators in bacteria, controls expression of several dozen genes during Streptomyces differentiation. Here, we report a novel function for the AdpA protein: inhibitor of chromosome replication at the initiation stage. AdpA specifically recognizes the 5′ region of the Streptomyces coelicolor replication origin ( oriC ). Our in vitro results show that binding of AdpA protein decreased access of initiator protein (DnaA) to the oriC region . We also found that mutation of AdpA-binding sequences increased the accessibility of oriC to DnaA, which led to more frequent replication and acceleration of Streptomyces differentiation (at the stage of aerial hyphae formation). Moreover, we also provide evidence that AdpA and DnaA proteins compete for oriC binding in an ATP-dependent manner, with low ATP levels causing preferential binding of AdpA, and high ATP levels causing dissociation of AdpA and association of DnaA. This would be consistent with a role for ATP levels in determining when aerial hyphae emerge.

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