scholarly journals The Rice Endosperm ADP-Glucose Pyrophosphorylase Large Subunit is Essential for Optimal Catalysis and Allosteric Regulation of the Heterotetrameric Enzyme

2014 ◽  
Vol 55 (6) ◽  
pp. 1169-1183 ◽  
Author(s):  
Aytug Tuncel ◽  
Joe Kawaguchi ◽  
Yasuharu Ihara ◽  
Hiroaki Matsusaka ◽  
Aiko Nishi ◽  
...  
FEBS Journal ◽  
2014 ◽  
Vol 281 (21) ◽  
pp. 4951-4963 ◽  
Author(s):  
Aytug Tuncel ◽  
Bilal Cakir ◽  
Seon-Kap Hwang ◽  
Thomas W. Okita

Plant Science ◽  
2016 ◽  
Vol 249 ◽  
pp. 70-83 ◽  
Author(s):  
Xiao-Jie Tang ◽  
Cheng Peng ◽  
Jie Zhang ◽  
Yue Cai ◽  
Xiao-Man You ◽  
...  

1999 ◽  
Vol 54 (5-6) ◽  
pp. 353-358 ◽  
Author(s):  
Leszek A. Kleszkowski ◽  
Lubomir N. Sokolov ◽  
Cheng Luo ◽  
Per Villand

Abstract A cDNA, A p L 1a , corresponding to a homologue of the large subunit of ADP-glucose pyrophosphorylase (AG Pase), has been isolated/characterised by screening a cDNA library prepared from leaves of Arabidopsis thaliana, followed by rapid amplification of cDNA 3′-ends (3′-RACE). Within the 1685 nucleotide-long sequence (excluding polyA tail), an open reading frame encodes a protein of 522 amino acids (aa), with a calculated molecular weight of 57.7 kDa. The derived aa sequence does not contain any discernible transit peptide cleavage site motif, similarly to two other recently sequenced full-length Arabidopsis homo-logues for AGPase, and shows ca. 58–78 % identity to homologous proteins from other plants/tissues. The corresponding gene was found (rosette and stem leaves, stems, flowers and fruits), consistent with its critical role in starch synthesis in


Plant Science ◽  
2005 ◽  
Vol 169 (5) ◽  
pp. 882-893 ◽  
Author(s):  
Jinpeng Xing ◽  
Xiangyang Li ◽  
Yuying Luo ◽  
Thomas J. Gianfagna ◽  
Harry W. Janes

2019 ◽  
Vol 10 ◽  
Author(s):  
Seon-Kap Hwang ◽  
Salvinder Singh ◽  
Jitendra Maharana ◽  
Samhita Kalita ◽  
Aytug Tuncel ◽  
...  

Genome ◽  
2016 ◽  
Vol 59 (7) ◽  
pp. 501-507 ◽  
Author(s):  
Xiao-Wei Zhang ◽  
Si-Yu Li ◽  
Ling-Ling Zhang ◽  
Qiang Yang ◽  
Qian-Tao Jiang ◽  
...  

ADP-glucose pyrophosphorylase (AGP), which consists of two large subunits (AGP-L) and two small subunits (AGP-S), controls the rate-limiting step in the starch biosynthetic pathway. In this study, a full-length open reading frame (ORF) of AGP-L gene (named as Agp2) in wheat and a series of Agp2 gene sequences in wheat relatives were isolated. The coding region of Agp2 contained 15 exons and 14 introns including a full-length ORF of 1566 nucleotides, and the deduced protein contained 522 amino acids (57.8 kDa). Generally, the phylogenetic tree of Agp2 indicated that sequences from A- and D-genome donor species were most similar to each other and sequences from B-genome donor species contained more variation. Starch accumulation and Agp2 expression in wheat grains reached their peak at 21 and 15 days post anthesis (DPA), respectively.


Planta ◽  
2006 ◽  
Vol 225 (4) ◽  
pp. 965-976 ◽  
Author(s):  
Eric D. Smidansky ◽  
Fletcher D. Meyer ◽  
Beth Blakeslee ◽  
Thaddeus E. Weglarz ◽  
Thomas W. Greene ◽  
...  

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.


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