scholarly journals Studies on Chlamydomonas chloroplast transformation: foreign DNA can be stably maintained in the chromosome.

1989 ◽  
Vol 1 (1) ◽  
pp. 123-132 ◽  
Author(s):  
A D Blowers ◽  
L Bogorad ◽  
K B Shark ◽  
J C Sanford
1989 ◽  
Vol 1 (1) ◽  
pp. 123 ◽  
Author(s):  
Alan D. Blowers ◽  
Lawrence Bogorad ◽  
Katherine B. Shark ◽  
John C. Sanford

1990 ◽  
Vol 79 (1) ◽  
pp. 184-189
Author(s):  
W. J. Lucas ◽  
A. Lansing ◽  
J. R. de Wet ◽  
V. Walbot

2020 ◽  
Vol 27 (2) ◽  
pp. 105-110 ◽  
Author(s):  
Niaz Ahmad ◽  
Muhammad Aamer Mehmood ◽  
Sana Malik

: In recent years, microalgae have emerged as an alternative platform for large-scale production of recombinant proteins for different commercial applications. As a production platform, it has several advantages, including rapid growth, easily scale up and ability to grow with or without the external carbon source. Genetic transformation of several species has been established. Of these, Chlamydomonas reinhardtii has become significantly attractive for its potential to express foreign proteins inexpensively. All its three genomes – nuclear, mitochondrial and chloroplastic – have been sequenced. As a result, a wealth of information about its genetic machinery, protein expression mechanism (transcription, translation and post-translational modifications) is available. Over the years, various molecular tools have been developed for the manipulation of all these genomes. Various studies show that the transformation of the chloroplast genome has several advantages over nuclear transformation from the biopharming point of view. According to a recent survey, over 100 recombinant proteins have been expressed in algal chloroplasts. However, the expression levels achieved in the algal chloroplast genome are generally lower compared to the chloroplasts of higher plants. Work is therefore needed to make the algal chloroplast transformation commercially competitive. In this review, we discuss some examples from the algal research, which could play their role in making algal chloroplast commercially successful.


2021 ◽  
Vol 319 ◽  
pp. 110677
Author(s):  
Meike M. de Boer ◽  
Shosha N.P. Wiznitzer ◽  
Peter J. van Koppen
Keyword(s):  

2014 ◽  
Vol 89 (4) ◽  
pp. 2287-2300 ◽  
Author(s):  
Yinghui Liu ◽  
Jianhua Li ◽  
Jieliang Chen ◽  
Yaming Li ◽  
Weixia Wang ◽  
...  

ABSTRACTThe cellular innate immune system recognizing pathogen infection is essential for host defense against viruses. In parallel, viruses have developed a variety of strategies to evade the innate immunity. The hepatitis B virus (HBV), a DNA virus that causes chronic hepatitis, has been shown to inhibit RNA helicase RIG-I-mediated interferon (IFN) induction. However, it is still unknown whether HBV could affect the host DNA-sensing pathways. Here we report that in transiently HBV-transfected Huh7 cells, the stably HBV-producing cell line HepAD38, and HBV-infected HepaRG cells and primary human hepatocytes, HBV markedly interfered with IFN-β induction and antiviral immunity mediated by the stimulator of interferon genes (STING), which has been identified as a central factor in foreign DNA recognition and antiviral innate immunity. Screening analysis demonstrated that the viral polymerase (Pol), but not other HBV-encoded proteins, was able to inhibit STING-stimulated interferon regulatory factor 3 (IRF3) activation and IFN-β induction. Moreover, the reverse transcriptase (RT) and the RNase H (RH) domains of Pol were identified to be responsible for the inhibitory effects. Furthermore, Pol was shown to physically associate with STING and dramatically decrease the K63-linked polyubiquitination of STING via its RT domain without altering the expression level of STING. Taken together, these observations suggest that besides its inherent catalytic function, Pol has a role in suppression of IFN-β production by direct interaction with STING and subsequent disruption of its K63-linked ubiquitination, providing a new mechanism for HBV to counteract the innate DNA-sensing pathways.IMPORTANCEAlthough whether and how HBV infection induces the innate immune responses are still controversial, it has become increasingly clear that HBV has developed strategies to counteract the pattern recognition receptor-mediated signaling pathways. Previous studies have shown that type I IFN induction activated by the host RNA sensors could be inhibited by HBV. However, it remains unknown whether HBV as a DNA virus utilizes evasion mechanisms against foreign DNA-elicited antiviral signaling. In recent years, the cytosolic DNA sensor and key adaptor STING has been demonstrated to be essential in multiple foreign DNA-elicited innate immune signalings. Here, for the first time, we report STING as a new target of HBV to antagonize IFN induction and identify the viral polymerase responsible for the inhibitory effect, thus providing an additional molecular mechanism by which HBV evades the innate immunity; this implies that in addition to its inherent catalytic function, HBV polymerase is a multifunctional immunomodulatory protein.


2014 ◽  
Vol 81 (1) ◽  
pp. 166-176 ◽  
Author(s):  
Francesca Bottacini ◽  
Mary O'Connell Motherway ◽  
Eoghan Casey ◽  
Brian McDonnell ◽  
Jennifer Mahony ◽  
...  

ABSTRACTBifidobacterium breveis a common and sometimes very abundant inhabitant of the human gut. Genome sequencing ofB. breveJCM 7017 revealed the presence of an extrachromosomal element, designated pMP7017 consisting of >190 kb, thus representing the first reported bifidobacterial megaplasmid.In silicocharacterization of this element revealed several genomic features supporting a stable establishment of the megaplasmid in its host, illustrated by predicted CRISPR-Cas functions that are known to protect the host against intrusion of foreign DNA. Interestingly, pMP7017 is also predicted to encode a conjugative DNA transfer apparatus and, consistent with this notion, we demonstrate here the conjugal transfer of pMP7017 to representative strains ofB. breveandB. longumsubsp.longum. We also demonstrate the presence of a megaplasmid with homology to pMP7017 in threeB. longumsubsp.longumstrains.


Cell ◽  
1989 ◽  
Vol 57 (5) ◽  
pp. 717-723 ◽  
Author(s):  
Marialuisa Lavitrano ◽  
Antonella Camaioni ◽  
Vito M. Fazio ◽  
Susanna Dolci ◽  
Maria G. Farace ◽  
...  

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