Effect of over-expression of phasin gene from<i>Aeromonas hydrophila</i>on biosynthesis of copolyesters of 3-hydroxybutyrate and 3-hydroxyhexanoate

Tian, Shujun; Lai, Weijian; Zheng, Zhong; Wang, Hexiang; Chen, Guoqiang

doi:10.1016/j.femsle.2005.01.020

Cited by 43 publications

(31 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Previous studies have indicated that PhaPs have an enhancing effect on PHA biosynthesis in vivo (9,10,24,25). To further investigate this effect, we performed in vitro polymerization activity assays in this study.…”

Section: Discussionmentioning

confidence: 99%

“…These observations include PhaP Ac expression leading to enhanced accumulation of PHA and/or altering the copolymer composition, likely by influencing the activity and substrate specificity of PhaC Ac (8,9). The same phenomenon was observed in recombinant bacteria between the PhaC and PhaP derived from Aeromonas hydrophila (10). However, these in vivo studies have not focused on the role of PhaP at the molecular level.…”

mentioning

confidence: 83%

See 1 more Smart Citation

Phasin Proteins Activate Aeromonas caviae Polyhydroxyalkanoate (PHA) Synthase but Not Ralstonia eutropha PHA Synthase

Ushimaru

Motoda

Numata

et al. 2014

Appl Environ Microbiol

View full text Add to dashboard Cite

bIn this study, we performed in vitro and in vivo activity assays of polyhydroxyalkanoate (PHA) synthases (PhaCs) in the presence of phasin proteins (PhaPs), which revealed that PhaPs are activators of PhaC derived from Aeromonas caviae (PhaC Ac ). In in vitro assays, among the three PhaCs tested, PhaC Ac was significantly activated when PhaPs were added at the beginning of polymerization (prepolymerization PhaC Ac ), whereas the prepolymerization PhaC Re (derived from Ralstonia eutropha) and PhaC Da (Delftia acidovorans) showed reduced activity with PhaPs. The PhaP-activated PhaC Ac showed a slight shift of substrate preference toward 3-hydroxyhexanoyl-CoA (C 6 ). PhaP Ac also activated PhaC Ac when it was added during polymerization (polymer-elongating PhaC Ac ), while this effect was not observed for PhaC Re . In an in vivo assay using Escherichia coli TOP10 as the host strain, the effect of PhaP Ac expression on PHA synthesis by PhaC Ac or PhaC Re was examined. As PhaP Ac expression increased, PHA production was increased by up to 2.3-fold in the PhaC Ac -expressing strain, whereas it was slightly increased in the PhaC Re -expressing strain. Taken together, this study provides evidence that PhaPs function as activators for PhaC Ac both in vitro and in vivo but do not activate PhaC Re . This activating effect may be attributed to the new role of PhaPs in the polymerization reaction by PhaC Ac .

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 83%

Phasin Proteins Activate Aeromonas caviae Polyhydroxyalkanoate (PHA) Synthase but Not Ralstonia eutropha PHA Synthase

Ushimaru

Motoda

Numata

et al. 2014

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…Furthermore, this phasin binds to DNA nonspecifically through a histone-like domain and plays a key role in intracellular localization and equal distribution of PHA granules to daughter cells during cell division (19,44). Last, PhaP from A. hydrophila (PhaP Ah ) was also observed to act as a positive regulator of the gene that encodes the PHA synthase in this organism, as the overexpression of phaP increased the expression of phaC (45).…”

Section: Role Of Phasins In Pha Metabolismmentioning

confidence: 99%

Phasins, Multifaceted Polyhydroxyalkanoate Granule-Associated Proteins

Mezzina

Pettinari

2016

Appl Environ Microbiol

103

View full text Add to dashboard Cite

Phasins are the major polyhydroxyalkanoate (PHA) granule-associated proteins. They promote bacterial growth and PHA synthesis and affect the number, size, and distribution of the granules. These proteins can be classified in 4 families with distinctive characteristics. Low-resolution structural studies and in silico predictions were performed in order to elucidate the structure of different phasins. Most of these proteins share some common structural features, such as a preponderant ␣-helix composition, the presence of disordered regions that provide flexibility to the protein, and coiled-coil interacting regions that form oligomerization domains. Due to their amphiphilic nature, these proteins play an important structural function, forming an interphase between the hydrophobic content of PHA granules and the hydrophilic cytoplasm content. Phasins have been observed to affect both PHA accumulation and utilization. Apart from their role as granule structural proteins, phasins have a remarkable variety of additional functions. Different phasins have been determined to (i) activate PHA depolymerization, (ii) increase the expression and activity of PHA synthases, (iii) participate in PHA granule segregation, and (iv) have both in vivo and in vitro chaperone activities. These properties suggest that phasins might play an active role in PHA-related stress protection and fitness enhancement. Due to their granule binding capacity and structural flexibility, several biotechnological applications have been developed using different phasins, increasing the interest in the study of these remarkable proteins.

show abstract

“…The results of reverse transcription-polymerase chain reaction suggested that phasin PhaP Ah , regulated phaC Ah gene at the transcription level. [31] Recombinant Ralstonia eutrophaPHB-4 harboring mutated PHA synthase genes phaC Ac from Aeromona caviae produced a PHA copolymer PHBHHx with 3.5 mol-% of 3HHx from soybean oil. When the mutants of phaC Ac gene were applied to this production system, the 3HHx fraction in copolymers varied in the range of 0-5.1 mol-%.…”

Section: Isolation Of Pha Synthases With Low Substrate Specificity Frmentioning

confidence: 99%

Metabolic Engineering for Microbial Production and Applications of Copolyesters Consisting of 3‐Hydroxybutyrate and Medium‐Chain‐Length 3‐Hydroxyalkanoates

Zou

Chen

2007

Macromolecular Bioscience

Self Cite

View full text Add to dashboard Cite

Poly(hydroxyalkanoate)s (PHAs) are a class of microbially synthesized polyesters that combine biological properties, such as biocompatibility and biodegradability, and non-bioproperties such as thermoprocessability, piezoelectricity, and nonlinear optical activity. PHA monomer structures and their contents strongly affect the PHA properties. Using metabolic engineering approaches, PHA structures and contents can be manipulated to achieve controllable monomer and PHA cellular contents. This paper focuses on metabolic engineering methods to produce PHA consisting of 3-hydroxybutyrate (3HB) and medium-chain-length 3-hydroxyalkanoates (3HA) in recombinant microbial systems. This type of copolyester has mechanical and thermal properties similar to conventional plastics such as poly(propylene) and poly(ethylene terephthalate) (PET). In addition, pathways containing engineered PHA synthases have proven to be useful for enhanced PHA production with adjustable PHA monomers and contents. The applications of PHA as implant biomaterials are briefly discussed here. In the very near term, metabolic engineering will help solve many problems in promoting PHA as a new type of plastic material for many applications.

show abstract

Effect of over-expression of phasin gene fromAeromonas hydrophilaon biosynthesis of copolyesters of 3-hydroxybutyrate and 3-hydroxyhexanoate

Cited by 43 publications

References 27 publications

Phasin Proteins Activate Aeromonas caviae Polyhydroxyalkanoate (PHA) Synthase but Not Ralstonia eutropha PHA Synthase

Phasin Proteins Activate Aeromonas caviae Polyhydroxyalkanoate (PHA) Synthase but Not Ralstonia eutropha PHA Synthase

Phasins, Multifaceted Polyhydroxyalkanoate Granule-Associated Proteins

Metabolic Engineering for Microbial Production and Applications of Copolyesters Consisting of 3‐Hydroxybutyrate and Medium‐Chain‐Length 3‐Hydroxyalkanoates

Contact Info

Product

Resources

About