Influence of the operon structure on poly(3-hydroxypropionate) synthesis in Shimwellia blattae

2014 ◽  
Vol 98 (17) ◽  
pp. 7409-7422 ◽  
Author(s):  
Björn Andreeßen ◽  
Benjamin Johanningmeier ◽  
Joachim Burbank ◽  
Alexander Steinbüchel
Keyword(s):  
Operon Structure

scholarly journals Opine-Based Agrobacterium Competitiveness: Dual Expression Control of the Agrocinopine Catabolism (acc) Operon by Agrocinopines and Phosphate Levels

2008 ◽  
Vol 190 (10) ◽  
pp. 3700-3711 ◽  
Author(s):  
H. Stanley Kim ◽  
Hyojeong Yi ◽  
Jaehee Myung ◽  
Kevin R. Piper ◽  
Stephen K. Farrand
Keyword(s):  
Plant Cells ◽  
Regulatory System ◽  
Food Sources ◽  
Competitive Environment ◽  
Operon Structure ◽  
Transcription Start ◽  
Transcription Start Sites ◽  
Expression Control ◽  
Maximum Utilization ◽  
Dual Expression

ABSTRACT Agrobacterium tumefaciens strain C58 can transform plant cells to produce and secrete the sugar-phosphate conjugate opines agrocinopines A and B. The bacterium then moves in response to the opines and utilizes them as exclusive sources of carbon, energy, and phosphate via the functions encoded by the acc operon. These privileged opine-involved activities contribute to the formation of agrobacterial niches in the environment. We found that the expression of the acc operon is induced by agrocinopines and also by limitation of phosphate. The main promoter is present in front of the first gene, accR, which codes for a repressor. This operon structure enables efficient repression when opine levels are low. The promoter contains two putative operators, one overlapping the −10 sequence and the other in the further upstream from it; two partly overlapped putative pho boxes between the two operators; and two consecutive transcription start sites. DNA fragments containing either of the operators bound purified repressor AccR in the absence of agrocinopines but not in the presence of the opines, demonstrating the on-off switch of the promoter. Induction of the acc operon can occur under low-phosphate conditions in the absence of agrocinopines and further increases when the opines also are present. Such opine-phosphate dual regulatory system of the operon may ensure maximum utilization of agrocinopines when available and thereby increase the chances of agrobacterial survival in the highly competitive environment with limited general food sources.

Operon Structure Optimization by Random Self-assembly

2009 ◽  
pp. 33-40
Author(s):  
Yusuke Nakagawa ◽  
Katsuyuki Yugi ◽  
Kenji Tsuge ◽  
Mitsuhiro Itaya ◽  
Hiroshi Yanagawa ◽  
...  
Keyword(s):  
Self Assembly ◽  
Structure Optimization ◽  
Operon Structure

Operon structure optimization by random self-assembly

2009 ◽  
Vol 9 (1) ◽  
pp. 173-181 ◽  
Author(s):  
Yusuke Nakagawa ◽  
Katsuyuki Yugi ◽  
Kenji Tsuge ◽  
Mitsuhiro Itaya ◽  
Hiroshi Yanagawa ◽  
...  
Keyword(s):  
Self Assembly ◽  
Structure Optimization ◽  
Operon Structure

scholarly journals Operon Structure and Regulation of the nos Gene Region of Pseudomonas stutzeri, Encoding an ABC-Type ATPase for Maturation of Nitrous Oxide Reductase

2003 ◽  
Vol 185 (6) ◽  
pp. 1895-1902 ◽  
Author(s):  
Ulrike Honisch ◽  
Walter G. Zumft
Keyword(s):  
Nitrous Oxide ◽  
Sequence Similarity ◽  
Pseudomonas Stutzeri ◽  
Soluble Form ◽  
Nitrous Oxide Reductase ◽  
Operon Structure ◽  
Catalytic Function ◽  
Enhanced Expression ◽  
Operon Expression

ABSTRACT The synthesis of a functional nitrous oxide reductase requires an assembly apparatus for the insertion of the prosthetic copper. Part of the system is encoded by maturation genes located in Pseudomonas stutzeri immediately downstream of the structural gene for the enzyme. We have studied the transcriptional organization and regulation of this region and found a nosDFYL tatE operon structure. In addition to a putative ABC transporter, consisting of NosD, NosF, and NosY, the operon encodes a Cu chaperone, NosL, and a component of the Tat translocon, TatE. The nosD operon was activated in response to anaerobiosis and nitrate denitrification. The membrane-bound regulator NosR was required for operon expression; in addition, DnrD, a regulator of the Crp-Fnr family, enhanced expression under anaerobic conditions. This establishes a likely signal transduction sequence of NO → DnrD → nosR/NosR → nosD operon. DnrD-dependent expression was also observed for the nnrS operon (located immediately downstream of the nosD operon), which encodes a putative heme-Cu protein (NnrS) and a member of the short-chain dehydrogenase family (ORF247). The NosF protein, encoded within the nosD operon, exhibits sequence similarity to ABC-type ATPases. It was fused to the Escherichia coli maltose-binding protein and overexpressed in soluble form. The fusion protein was purified and shown to have ATPase activity. NosF is the first maturation factor for which a catalytic function has been demonstrated in vitro.

scholarly journals The Adherence-Associated Lipoprotein P100, Encoded by an opp Operon Structure, Functions as the Oligopeptide-Binding Domain OppA of a Putative Oligopeptide Transport System in Mycoplasma hominis

1999 ◽  
Vol 181 (16) ◽  
pp. 4873-4878 ◽  
Author(s):  
Birgit Henrich ◽  
Miriam Hopfe ◽  
Annette Kitzerow ◽  
Ulrich Hadding
Keyword(s):  
Transport System ◽  
Peptide Binding ◽  
Mycoplasma Hominis ◽  
Initiation Site ◽  
Genomic Region ◽  
Binding Domain ◽  
Terminal Region ◽  
Peptide Transport ◽  
Operon Structure ◽  
Active Transport System

ABSTRACT Mycoplasma hominis, a cell-wall-less prokaryote, was shown to be cytoadherent by the participation of a 100-kDa membrane protein (P100). To identify the gene encoding P100, peptides of P100 were partially sequenced to enable the synthesis of P100-specific oligonucleotides suitable as probes for the detection of the P100 gene. With this strategy, we identified a genomic region of about 10.4 kb inM. hominis FBG carrying the P100 gene. Analysis of the complete deduced protein sequence suggests that P100 is expressed as a pre-lipoprotein with a structure in the N-terminal region common to peptide-binding proteins and an ATP- or GTP-binding P-loop structure in the C-terminal region. Downstream of the P100 gene, an additional four open reading frames putatively encoding the four core domains of an active transport system, OppBCDF, were localized. The organization of the P100 gene and oppBCDF in a transcriptionally active operon structure was demonstrated in Northern blot and reverse transcription-PCR analyses, as all gene-specific probes detected a common RNA of 9.5 kb. Primer extension analysis revealed that the transcriptional initiation site was localized 323 nucleotides upstream of the methionine-encoding ATG of the P100 gene. The peptide-binding character of the P100 protein was confirmed by fluorescence spectroscopy and strongly suggests that the cytoadherence-mediating lipoprotein P100 represents OppA, the substrate-binding domain of a peptide transport system in M. hominis.

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