The development of plants an introduction to plant cell development. By Jeremy Burgess. Cambridge University Press, 1985. Pp. 246. £27.50 hardback, £9.95 paperback

BioEssays ◽  
1986 ◽  
Vol 4 (5) ◽  
pp. 234-234
Author(s):  
Paul B. Green
2019 ◽  
Vol 157 ◽  
pp. 157-161 ◽  
Author(s):  
Elizabeth Kordyum ◽  
David Chapman ◽  
Vasyl Brykov

2007 ◽  
Vol 51 (5) ◽  
pp. 751-762 ◽  
Author(s):  
Julia Legen ◽  
Gerhard Wanner ◽  
Reinhold G. Herrmann ◽  
Ian Small ◽  
Christian Schmitz-Linneweber

2003 ◽  
Vol 16 (2) ◽  
pp. 123-131 ◽  
Author(s):  
Elizabeth A. Doyle ◽  
Kris N. Lambert

Root-knot nematodes are obligate plant parasites that alter plant cell growth and development by inducing the formation of giant cells for feeding. Nematodes inject secretions from their esophageal glands through their stylet and into plant cells to induce giant cell formation. Meloidogyne javanica chorismate mutase 1 (MjCM-1) is one such esophageal gland protein likely to be secreted from the nematode as giant cells form. MjCM-1 has two domains, an N-terminal chorismate mutase (CM) domain and a C-terminal region of unknown function. It is the N-terminal CM domain of the protein that is the predominant form produced in root-knot nematodes. Transgenic expression of MjCM-1 in soybean hairy roots results in a phenotype of reduced and aborted lateral roots. Histological studies demonstrate the absence of vascular tissue in hairy roots expressing MjCM-1. The phenotype of MjCM-1 expressed at low levels can be rescued by the addition of indole-3-acetic acid (IAA), indicating MjCM-1 overexpression reduces IAA biosynthesis. We propose MjCM-1 lowers IAA by causing a competition for chorismate, resulting in an alteration of chorismate-derived metabolites and, ultimately, in plant cell development. Therefore, we hypothesize that MjCM-1 is involved in allowing nematodes to establish a parasitic relationship with the host plant.


1992 ◽  
Vol 95 (1/2) ◽  
pp. 50 ◽  
Author(s):  
James A. Guikema ◽  
Greg L. Gallegos

1988 ◽  
Vol 253 (3) ◽  
pp. 795-800 ◽  
Author(s):  
R E Campbell ◽  
C T Brett ◽  
J R Hillman

A particulate enzyme preparation made from suspension-cultured dwarf-French-bean (Phaseolus vulgaris) cv. Canadian Wonder cells was shown to incorporate xylose from UDP-D-[14C]xylose into polysaccharide. The reaction was dependent upon the presence of UDP-D-glucose and was stimulated, and apparently protected, by GDP-D-glucose and GDP-D-mannose, though neither was able to replace UDP-D-glucose as a glycosyl donor. The product of the reaction was identified as xyloglucan by analysis of products of enzyme breakdown and acid hydrolysis. Mr determination after proteinase K digestion indicated that the nascent xyloglucan is closely associated with protein. Preincubation of the enzyme with UDP-D-glucose stimulated incorporation from UDP-D-[14C]xylose, suggesting an ‘imprecise’ mechanism of biosynthesis, as defined by Waldron & Brett [(1985) in Biochemistry of Plant Cell Walls (Brett, C. T. & Hillman, J. R., eds.) (SEB Semin. Ser. 28), pp. 79-97, Cambridge University Press, Cambridge].


1986 ◽  
Vol 61 (4) ◽  
pp. 535-535
Author(s):  
William Newcomb
Keyword(s):  

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