Construction of Shuttle Plasmids Which Can Be Efficiently Mobilized from Escherichia coli into the Chromatically Adapting Cyanobacterium, Fremyella diplosiphon

Cobley, John G.; Zerweck, E.; Reyes, Rebecca; Mody, Anahita Minoo; Seludo-Unson, J. Racquel G; Jaeger, H; Weerasuriya, Siromi; Navankasattusas, Sutip

doi:10.1006/plas.1993.1037

Cited by 91 publications

(76 citation statements)

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“…Fremyella diplosiphon strain SF33 (Cobley et al, 1993), which we use as a wild-type (WT) pigmentation strain, and the DtonB mutant were grown as described previously (Bordowitz & Montgomery, 2008). For ironlimited medium (BG11 -Fe ), ammonium citrate replaced ferric ammonium citrate in BG11 and the water used for the medium was run through Chelex-100 resin (Bio-Rad) to eliminate traces of iron (Sherman & Sherman, 1983).…”

Section: Methodsmentioning

confidence: 99%

“…Overnight-grown E. coli strains and a culture of F. diplosiphon at an OD 750 of~0.1 were utilized for the mating process. Initial transconjugants were selected by screening for resistance to 10 mg neomycin ml 21 with growth on nitrocellulose membrane layered on medium D plates as previously described (Cobley et al, 1993(Cobley et al, , 2002. Colonies selected from the plates were grown in BG11 medium with 10 mg neomycin ml 21 for the first selection.…”

Section: Methodsmentioning

confidence: 99%

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FdTonB is involved in the photoregulation of cellular morphology during complementary chromatic adaptation in Fremyella diplosiphon

Pattanaik

Montgomery

2010

Microbiology

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We have characterized a Fremyella diplosiphon TonB protein (FdTonB) and investigated its function during complementary chromatic adaptation. Sequence similarity analysis of FdTonB (571 aa) led to identification of several conserved domains characteristic of TonB proteins, including an N-terminal transmembrane domain, a central proline-rich spacer and a C-terminal TonB-related domain (TBRD). We identified a novel glycine-rich domain containing (Gly-X) n repeats. To assess FdTonB function, we constructed a DtonB mutant through homologous recombination based upon truncation of the central proline-rich spacer, glycine-rich domain and TBRD. Our DtonB mutant exhibited an aberrant cellular morphology under green light, with expanded cell width compared to the parental wild-type (WT) strain. The cellular morphology of the DtonB mutant recovered upon WT tonB expression. Interestingly, tonB expression was found to be independent of RcaE. As DtonB and WT strains respond in the same way when grown under iron-replete versus iron-limited conditions, our results suggest that FdTonB is not involved in the classic TonB function of mediating cellular adaptation to iron limitation, but exhibits a novel function related to the photoregulation of cellular morphology in F. diplosiphon.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

FdTonB is involved in the photoregulation of cellular morphology during complementary chromatic adaptation in Fremyella diplosiphon

Pattanaik

Montgomery

2010

Microbiology

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“…PCC 7601 (also known as Calothrix sp. and Fremyella diplosiphon UTEX 481) and SF33 (a derivative of the latter: Cobley et al, 1993), are unable to form functional heterocysts. They were grown axenically in BG-11 liquid medium (nitrate-containing; Rippka, 1988) supplemented with 10 mM NaHCO 3, bubbled with wet air (10 l min 21 ) enriched to 1 % (v/v) CO 2 and illuminated by cool-white fluorescent light (25 mmol m 22 s 21 ).…”

Section: Methodsmentioning

confidence: 99%

“…Tolypothrix sp. PCC 7601 and its SF33 mutant derivative that makes shorter filaments (Cobley et al, 1993) bleach if deprived of exogenous combined nitrogen source. In contrast, strain PCC 7601/1 is able to differentiate fully functional heterocysts, and thus grows under aerobic N 2 -fixing conditions.…”

Section: Expression Of Nblaimentioning

confidence: 99%

Immunolocalization of NblA, a protein involved in phycobilisome turnover, during heterocyst differentiation in cyanobacteria

Alda¹,

Lichtlé²,

Thomas³

et al. 2004

Microbiology

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In unicellular non-diazotrophic cyanobacteria, NblA is a small polypeptide required for phycobilisome degradation during macronutrient limitation. In the filamentous N2-fixing Tolypothrix sp., a nblA gene (nblAI) lies upstream of the cpeBA operon that encodes phycoerythrin apoproteins. Using a specific anti-NblAI antibody it was found that in strains of Tolypothrix sp. NblAI abundance increases under nitrogen-limiting conditions but the protein is also present in cells grown in nitrogen-replete medium. Gold immunolabelling experiments showed that, upon a nitrogen shift-down, NblAI is preferentially located in the differentiated heterocysts, where O2 evolution has to be shut off for nitrogenase to operate. The results lead to the proposal that NblAI is a necessary ‘cofactor’ but not the triggering factor that governs phycobilisome degradation in Tolypothrix sp.

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“…John Cobley had generated an F. diplosiphon mutant that grew as short filaments such that the colonies formed by the cells remained discrete (the filaments did not quickly spread over the entire plate). Furthermore, John constructed a plasmid that could autonomously replicate in F. diplosiphon, facilitating the stable introduction of DNA into the organism (Cobley et al 1993). We used these tools to complement the FdR mutant and identified the gene rcaC (Chiang et al 1992).…”

Section: Use Of Mutants and Genetic Techniques To Dissect Complementamentioning

confidence: 99%

A molecular understanding of complementary chromatic adaptation

Grossman

Discoveries in Photosynthesis

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Photosynthetic activity and the composition of the photosynthetic apparatus are strongly regulated by environmental conditions. Some visually dramatic changes in pigmentation of cyanobacterial cells that occur during changing nutrient and light conditions reflect marked alterations in components of the major light-harvesting complex in these organisms, the phycobilisome. As noted well over 100 years ago, the pigment composition of some cyanobacteria is very sensitive to ambient wavelengths of light; this sensitivity reflects molecular changes in polypeptide constituents of the phycobilisome. The levels of different pigmented polypeptides or phycobiliproteins that become associated with the phycobilisome are adjusted to optimize absorption of excitation energy present in the environment. This process, called complementary chromatic adaptation, is controlled by a bilin-binding photoreceptor related to phytochrome of vascular plants; however, many other regulatory elements also play a role in chromatic adaptation. My perspectives and biases on the history and significance of this process are presented in this essay.

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Construction of Shuttle Plasmids Which Can Be Efficiently Mobilized from Escherichia coli into the Chromatically Adapting Cyanobacterium, Fremyella diplosiphon

Cited by 91 publications

References 0 publications

FdTonB is involved in the photoregulation of cellular morphology during complementary chromatic adaptation in Fremyella diplosiphon

FdTonB is involved in the photoregulation of cellular morphology during complementary chromatic adaptation in Fremyella diplosiphon

Immunolocalization of NblA, a protein involved in phycobilisome turnover, during heterocyst differentiation in cyanobacteria

A molecular understanding of complementary chromatic adaptation

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