Identification and characterization of Arabidopsis thaliana genes involved in xylem secondary cell walls

2006 ◽  
Vol 119 (3) ◽  
pp. 189-194 ◽  
Author(s):  
Ryusuke Yokoyama ◽  
Kazuhiko Nishitani
2010 ◽  
Vol 27 (3) ◽  
pp. 259-266 ◽  
Author(s):  
Hitomi Ichinose ◽  
Nobuyuki Nishikubo ◽  
Taku Demura ◽  
Satoshi Kaneko

Science ◽  
2013 ◽  
Vol 341 (6150) ◽  
pp. 1103-1106 ◽  
Author(s):  
Ruben Vanholme ◽  
Igor Cesarino ◽  
Katarzyna Rataj ◽  
Yuguo Xiao ◽  
Lisa Sundin ◽  
...  

Lignin is a major component of plant secondary cell walls. Here we describe caffeoyl shikimate esterase (CSE) as an enzyme central to the lignin biosynthetic pathway. Arabidopsis thaliana cse mutants deposit less lignin than do wild-type plants, and the remaining lignin is enriched in p-hydroxyphenyl units. Phenolic metabolite profiling identified accumulation of the lignin pathway intermediate caffeoyl shikimate in cse mutants as compared to caffeoyl shikimate levels in the wild type, suggesting caffeoyl shikimate as a substrate for CSE. Accordingly, recombinant CSE hydrolyzed caffeoyl shikimate into caffeate. Associated with the changes in lignin, the conversion of cellulose to glucose in cse mutants increased up to fourfold as compared to that in the wild type upon saccharification without pretreatment. Collectively, these data necessitate the revision of currently accepted models of the lignin biosynthetic pathway.


Planta ◽  
2000 ◽  
Vol 211 (2) ◽  
pp. 256-264 ◽  
Author(s):  
Raynald Girault ◽  
Isabelle His ◽  
Christine Andeme-Onzighi ◽  
Azeddine Driouich ◽  
Claudine Morvan

2010 ◽  
Vol 22 (12) ◽  
pp. 4084-4097 ◽  
Author(s):  
Kentaro Tamura ◽  
Yoichiro Fukao ◽  
Masaaki Iwamoto ◽  
Tokuko Haraguchi ◽  
Ikuko Hara-Nishimura

1999 ◽  
Vol 65 (2) ◽  
pp. 569-577 ◽  
Author(s):  
Michelle M. Sheehan ◽  
Elizabeth Stanley ◽  
Gerald F. Fitzgerald ◽  
Douwe van Sinderen

A lysis module encoded by the temperate bacteriophage φO1205 was identified. This lysis module contains a lysin gene, designatedlyt51, and two putative holin-encoding genes, designatedlyt49 and lyt50. lyt51 encodes a lytic enzyme specifically directed against streptococcal cell walls. Similar to other phage-encoded lysins, Lyt51 appears to have a modular design in which the N-terminal portion corresponds to its enzymatic activity while the C-terminal region is responsible for its substrate binding specificity. The two putative holin-encoding genes,lyt49 and lyt50, located immediately upstream of lyt51, were identified on the basis of their homology to other identified holin-encoding genes. Expression of lyt49 or lyt50 in Escherichia coli was shown to cause cell death and leakage of the intracellular enzyme isocitrate dehydrogenase into the growth medium without apparent lysis of the cells. Southern blotting experiments demonstrated that at least one of the three components of the identified lysis module is present in all members of a large collection of bacteriophages, indicating that components of this lysis module are widespread among bacteriophages infecting Streptococcus thermophilus.


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