scholarly journals Inhibition of Starch Biosynthesis by Antisense Expression of cDNAs Encoding ADP-Glucose Pyrophosphorylase Small Subunit in Sweetpotato

2007 ◽  
Vol 34 (4) ◽  
pp. 277-283
Author(s):  
Sung-Ran Min ◽  
Jung-Myung Bae ◽  
Chee-Hark Harn ◽  
Won-Joong Jeong ◽  
Young-Bok Lee ◽  
...  
2003 ◽  
Vol 131 (2) ◽  
pp. 684-696 ◽  
Author(s):  
Philip E. Johnson ◽  
Nicola J. Patron ◽  
Andrew R. Bottrill ◽  
Jason R. Dinges ◽  
Brendan F. Fahy ◽  
...  

Gene ◽  
2004 ◽  
Vol 339 ◽  
pp. 173-180 ◽  
Author(s):  
Seol Ah Noh ◽  
Man Sup Kwak ◽  
Haeng Soon Lee ◽  
Gyung Hye Huh ◽  
Jang Ryol Liu ◽  
...  

1984 ◽  
Vol 74 (2) ◽  
pp. 424-429 ◽  
Author(s):  
William H. Outlaw ◽  
Mitchell C. Tarczynski

2001 ◽  
Vol 158 (10) ◽  
pp. 1273-1279 ◽  
Author(s):  
Jung M. Bae ◽  
Chee H. Harn ◽  
Kyoung H. Tae ◽  
Mi C. Suh ◽  
Jeong S. Shin ◽  
...  

2012 ◽  
Vol 69 (6) ◽  
pp. 1077-1093 ◽  
Author(s):  
Benjamin Faix ◽  
Volodymyr Radchuk ◽  
Annika Nerlich ◽  
Christine Hümmer ◽  
Ruslana Radchuk ◽  
...  

1994 ◽  
Vol 49 (3-4) ◽  
pp. 215-219 ◽  
Author(s):  
Per Villand ◽  
Leszek A. Kleczkowski

A hypothesis is presented concerning a putative extra-am yloplastic location of barley seed endosperm ADP-glucose pyrophosphorylase (AGPase), a key enzyme of starch biosynthesis. The hypothesis is based both on indirect and direct evidence obtained in our laboratory as well as on data of other investigators. It is proposed that ADP-glucose form ed by the extraamyloplastic enzyme is transported to the am yloplasts via an ADP-glucose carrier in the plastid membrane, and then is utilized by the starch biosynthesizing machinery of these organelles. In addition to the extra-am yloplastic form of AGPase, barley endosperm contains also a second isozyme of AGPase, located in the amyloplasts. Presence of isozymes of AGPase in cereal seed endosperm is consistent with biochemical, molecular and genetic data on starch biosynthesis in this tissue


2007 ◽  
Vol 34 (6) ◽  
pp. 480 ◽  
Author(s):  
Sandrine Rösti ◽  
Brendan Fahy ◽  
Kay Denyer

A mutant of rice was identified with a Tos17 insertion in OsAPL1, a gene encoding a large subunit (LSU) of ADP-glucose pyrophosphorylase (AGPase). The insertion prevents production of a normal transcript from OsAPL1. Characterisation of the mutant (apl1) showed that the LSU encoded by OsAPL1 is required for AGPase activity in rice leaf blades. In mutant leaf blades, the AGPase small subunit protein is not detectable and the AGPase activity and starch content are reduced to <1 and <5% of that in wild type blades, respectively. The mutation also leads to a reduction in starch content in the leaf sheaths but does not significantly affect AGPase activity or starch synthesis in other parts of the plant. The sucrose, glucose and fructose contents of the leaves are not affected by the mutation. Despite the near absence of starch in the leaf blades, apl1 mutant rice plants grow and develop normally under controlled environmental conditions and show no reduction in productivity.


Sign in / Sign up

Export Citation Format

Share Document