http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Paik, Sang-Min,Kim, Joonwon,Jin, EonSeon,Jeon, Noo Li Elsevier 2019 Bioresource technology Vol.272 No.-
<P><B>Abstract</B></P> <P>High uptake of malate and efficient distribution of intracellular malate to organelles contributed to biomass increase, reducing maintenance energy. In this study, transgenic <I>Chlamydomonas reinhardtii</I> was developed that stably expresses malate synthase in the chloroplast. The strains under glyoxylate treatment showed 19% more increase in microalgal biomass than wild-type. By RNA analysis, transcript levels of malate dehydrogenase (<I>MDH4</I>) and acetyl-CoA synthetase (<I>ACS3</I>), isocitrate lyase (<I>ICL1</I>) and malate synthase (<I>MAS1</I>), were significantly more expressed (17%, 42%, 24%, and 18% respectively), which was consistent with reported heterotrophic metabolism flux analysis with the objective function maximizing biomass. Photosynthetic F<SUB>v</SUB>/F<SUB>m</SUB> was slightly reduced. A more meticulous analysis is necessary, but, in the transgenic microalgae with malate synthase overexpression, the metabolism is likely to more rely on heterotrophic energy production via TCA cycle and glyoxylate shunt than on photosynthesis, resulting in the increase in microalgal biomass.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Chloroplastic transgenic <I>C. reinhardtii</I> was developed that stably expressed malate synthase. </LI> <LI> This transgenic strain showed a more 19% increase in dry cell weight than wild-type strain. </LI> <LI> Transcripts of <I>MDH4</I>, <I>ACS3</I>, <I>ICL1</I>, and <I>MAS1</I> were increased, and F<SUB>v</SUB>/F<SUB>m</SUB> was decreased. </LI> <LI> Upregulation of heterotrophic metabolism might be involved in biomass increase. </LI> <LI> This could serve as a valuable strain for treating wastewater containing acetate and glyoxylate. </LI> </UL> </P>
Molecular Characterization of AceB, a Gene Encoding Malate Synthase in Corynebacterium glutamicum
LEE, HEUNG-SHICK,SINSKEY, ANTHONY J. 한국미생물 · 생명공학회 1994 Journal of microbiology and biotechnology Vol.4 No.4
The aceB gene, encoding for malate synthase, one of the key enzymes of glyoxylate bypass, was isolated from a pMT1-based Corynebacterium glutamicum gene library via complementation of an Escherichia coli aceB mutant on an acetate minimal medium. The aceB gene was closely linked to aceA, separated by 598 base pairs, and transcribed in divergent direction. The aceB expressed a protein product of Mr 83,000 in Corynebacterium glutamicum which was unusually large compared with those of other malate synthases. A DNA-sequence analysis of the cloned DNA identified an open-reading frame of 2,217 base pairs which encodes a protein with the molecular weight of 82,311 comprising 739 amino acids. The putative protein product showed only limited amino acid-sequence homology to its counterparts in other organisms. The N-terminal region of the protein, which shows no apparent homology with the known sequences of other malate synthases, appeared to be responsible for the protein's unusually large size. A potential calciumbinding domain of EF-hand structure found among eukaryotes was detected in the N-terminal region of the deduced protein.