scholarly journals Interaction of the Nitrogen Regulatory Protein GlnB (PII) with Biotin Carboxyl Carrier Protein (BCCP) Controls Acetyl-CoA Levels in the Cyanobacterium Synechocystis sp. PCC 6803

2016 ◽  
Vol 7 ◽  
Author(s):  
Waldemar Hauf ◽  
Katharina Schmid ◽  
Edileusa C. M. Gerhardt ◽  
Luciano F. Huergo ◽  
Karl Forchhammer
Keyword(s):  
Regulatory Protein ◽  
Carrier Protein ◽  
Acetyl Coa ◽  
Biotin Carboxyl Carrier Protein ◽  
Synechocystis Sp ◽  
Pcc 6803

scholarly journals The Acyl-Acyl Carrier Protein Synthetase from Synechocystis sp. PCC 6803 Mediates Fatty Acid Import

2012 ◽  
Vol 159 (2) ◽  
pp. 606-617 ◽  
Author(s):  
Simon von Berlepsch ◽  
Hans-Henning Kunz ◽  
Susanne Brodesser ◽  
Patrick Fink ◽  
Kay Marin ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Synechocystis Sp ◽  
Pcc 6803

Use of 13C in biosynthetic studies. The labeling pattern in dihydrofusarubin enriched from [13C]- and [13C, 2H]acetate in cultures of Fusarium solani

1980 ◽  
Vol 58 (13) ◽  
pp. 1380-1385 ◽  
Author(s):  
Itsuo Kurobane ◽  
Leo C. Vining ◽  
A. Gavin McInnes ◽  
John A. Walter
Keyword(s):  
Fusarium Solani ◽  
Carrier Protein ◽  
Single Chain ◽  
Acetyl Coa ◽  
Biotin Carboxyl Carrier Protein ◽  
H Nmr ◽  
Malonyl Coa ◽  
Starter Unit ◽  
Biosynthetic Studies ◽  
Labeling Pattern

The pattern of 13C and 2H incorporation from [1-13C]-, [2-13C]-, [1-13C0;1;1,2-13C1;0;1]-, and [2-13C0;1,2-2H3;3]acetate into dihydrofusarubin 1, produced by cultures of Fusariumsolani, has been determined by 13C and 2H nmr of the derivatives anhydrofusarubin 3 and anhydrofusarubin diacetate 4. The results show that 1 is biosynthesized from seven uniformly-incorporated acetate units with C-3, C-11 originating from the "starter" unit. They strongly suggest that linear head-to-tail condensation of an acetate and six malonate units forms a single-chain heptaketide intermediate. The evidence also suggests that, during conversion of [13C, 2H]-labeled acetyl-CoA to malonyl-CoA, 2H is transferred to biotin carboxyl carrier protein where it does not exchange rapidly with the medium and is available for conversion of endogenous malonyl-CoA to [2H]-enriched acetyl-CoA.

scholarly journals The Three-Dimensional Structure of the Biotin Carboxylase-Biotin Carboxyl Carrier Protein Complex of E. coli Acetyl-CoA Carboxylase

Structure ◽  
2013 ◽  
Vol 21 (4) ◽  
pp. 650-657 ◽  
Author(s):  
Tyler C. Broussard ◽  
Matthew J. Kobe ◽  
Svetlana Pakhomova ◽  
David B. Neau ◽  
Amanda E. Price ◽  
...  
Keyword(s):  
Protein Complex ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Carrier Protein ◽  
Biotin Carboxylase ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Biotin Carboxyl Carrier Protein ◽  
Three Dimensional Structure ◽  
E Coli

scholarly journals Maximizing PHB content in Synechocystis sp. PCC 6803: development of a new photosynthetic overproduction strain

2020 ◽  
Author(s):  
Moritz Koch ◽  
Jonas Bruckmoser ◽  
Jörg Scholl ◽  
Waldemar Hauf ◽  
Bernhard Rieger ◽  
...  
Keyword(s):  
Industrial Production ◽  
Regulatory Protein ◽  
Continuous Light ◽  
Dry Weight ◽  
History Of ◽  
Model Strain ◽  
Synechocystis Sp ◽  
Rapid Conversion ◽  
Production Strain ◽  
Pcc 6803

AbstractPHB (poly-hydroxy-butyrate) represents a promising bioplastic variety with good biodegradation properties. Furthermore, PHB can be produced completely carbon-neutral when synthesized in the natural producer cyanobacterium Synechocystis sp. PCC 6803. This model strain has a long history of various attempts to further boost its low amounts of produced intracellular PHB of ~15 % per cell-dry-weight (CDW).We have created a new strain that lacks the regulatory protein PirC (gene product of sll0944), which causes a rapid conversion of the intracellular glycogen pools to PHB under nutrient limiting conditions. To further improve the intracellular PHB content, two genes from the PHB metabolism, phaA and phaB from the known production strain Cupriavidus necator, were introduced under the regime of the strong promotor PpsbA2. The created strain, termed PPT1 (Δsll0944-REphaAB), produced high amounts of PHB under continuous light as well under day-night rhythm. When grown in nitrogen and phosphor depleted medium, the cells produced up to 63 % / CDW. Upon the addition of acetate, the content was further increased to 81 % / CDW. The produced polymer consists of pure PHB, which is highly isotactic.The achieved amounts were the highest ever reported in any known cyanobacterium and demonstrate the potential of cyanobacteria for a sustainable, industrial production of PHB.

scholarly journals Maximizing PHB content in Synechocystis sp. PCC 6803: a new metabolic engineering strategy based on the regulator PirC

2020 ◽  
Vol 19 (1) ◽  
Author(s):  
Moritz Koch ◽  
Jonas Bruckmoser ◽  
Jörg Scholl ◽  
Waldemar Hauf ◽  
Bernhard Rieger ◽  
...  
Keyword(s):  
Regulatory Protein ◽  
Continuous Light ◽  
Dry Weight ◽  
Model System ◽  
Phosphoglycerate Mutase ◽  
Producer Strain ◽  
Nitrogen And Phosphorus ◽  
Engineering Strategy ◽  
Synechocystis Sp ◽  
Pcc 6803

Abstract Background PHB (poly-hydroxy-butyrate) represents a promising bioplastic alternative with good biodegradation properties. Furthermore, PHB can be produced in a completely carbon–neutral fashion in the natural producer cyanobacterium Synechocystis sp. PCC 6803. This strain has been used as model system in past attempts to boost the intracellular production of PHB above ~ 15% per cell-dry-weight (CDW). Results We have created a new strain that lacks the regulatory protein PirC (product of sll0944), which exhibits a higher activity of the phosphoglycerate mutase resulting in increased PHB pools under nutrient limiting conditions. To further improve the intracellular PHB content, two genes involved in PHB metabolism, phaA and phaB, from the known producer strain Cupriavidus necator, were introduced under the control of the strong promotor PpsbA2. The resulting strain, termed PPT1 (ΔpirC-REphaAB), produced high amounts of PHB under continuous light as well under a day-night regime. When grown in nitrogen and phosphorus depleted medium, the cells produced up to 63% per CDW. Upon the addition of acetate, the content was further increased to 81% per CDW. The produced polymer consists of pure PHB, which is highly isotactic. Conclusion The amounts of PHB achieved with PPT1 are the highest ever reported in any known cyanobacterium and demonstrate the potential of cyanobacteria for a sustainable, industrial production of PHB.

scholarly journals Biotin carboxyl carrier protein and carboxyltransferase subunits of the multi-subunit form of acetyl-CoA carboxylase from Brassica napus: cloning and analysis of expression during oilseed rape embryogenesis

1996 ◽  
Vol 315 (1) ◽  
pp. 103-112 ◽  
Author(s):  
Kieran M. ELBOROUGH ◽  
Robert WINZ ◽  
Ranjit K. DEKA ◽  
Jonathan E. MARKHAM ◽  
Andrew J. WHITE ◽  
...  
Keyword(s):  
Brassica Napus ◽  
Embryo Development ◽  
Oilseed Rape ◽  
Northern Analysis ◽  
Carrier Protein ◽  
Type I ◽  
Type Ii ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Biotin Carboxyl Carrier Protein

In the oilseed rape Brassica napus there are two forms of acetyl-CoA carboxylase (ACCase). As in other dicotyledonous plants there is a type I ACCase, the single polypeptide 220 kDa form, and a type II multi-subunit complex analogous to that of Escherichia coli and Anabaena. This paper describes the cloning and characterization of a plant biotin carboxyl carrier protein (BCCP) from the type II ACCase complex that shows 61% identity/79% similarity with Anabaena BCCP at the amino acid level. Six classes of nuclear encoded oilseed rape BCCP cDNA were cloned, two of which contained the entire coding region. The BCCP sequences allowed the assignment of function to two previously unassigned Arabidopsis expressed sequence tag (EST) sequences. We also report the cloning of a second type II ACCase component from oilseed rape, the β-carboxyltransferase subunit (βCT), which is chloroplast-encoded. Northern analysis showed that although the relative levels of BCCP and βCT mRNA differed between different oilseed rape tissues, their temporal patterns of expression were identical during embryo development. At the protein level, expression of BCCP during embryo development was studied by Western blotting, using affinity-purified anti-biotin polyclonal sera. With this technique a 35 kDa protein thought to be BCCP was shown to reside within the chloroplast. This analysis also permitted us to view the differential expression of several unidentified biotinylated proteins during embryogenesis.

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