scholarly journals ADP-Glucose Pyrophosphorylase Large Subunit cDNA from Barley Endosperm

1992 ◽  
Vol 100 (3) ◽  
pp. 1617-1618 ◽  
Author(s):  
Per Villand ◽  
Odd-Arne Olsen ◽  
Andrzej Kilian ◽  
Leszek A. Kleczkowski
Keyword(s):  
Large Subunit ◽  
Barley Endosperm ◽  
Adp Glucose Pyrophosphorylase

Molecular Cloning and Spatial Expression of an ApL1 cDNA for the Large Subunit of ADP-Glucose Pyrophosphorylase from Arabidopsis thaliana

1999 ◽  
Vol 54 (5-6) ◽  
pp. 353-358 ◽  
Author(s):  
Leszek A. Kleszkowski ◽  
Lubomir N. Sokolov ◽  
Cheng Luo ◽  
Per Villand
Keyword(s):  
Arabidopsis Thaliana ◽  
Large Subunit ◽  
Critical Role ◽  
Starch Synthesis ◽  
Transit Peptide ◽  
Homologous Proteins ◽  
Peptide Cleavage ◽  
Reading Frame ◽  
Calculated Molecular Weight ◽  
Adp Glucose Pyrophosphorylase

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

Isolation and expression analysis of two tomato ADP-glucose pyrophosphorylase S (large) subunit gene promoters

Plant Science ◽  
2005 ◽  
Vol 169 (5) ◽  
pp. 882-893 ◽  
Author(s):  
Jinpeng Xing ◽  
Xiangyang Li ◽  
Yuying Luo ◽  
Thomas J. Gianfagna ◽  
Harry W. Janes
Keyword(s):  
Expression Analysis ◽  
Large Subunit ◽  
Gene Promoters ◽  
Subunit Gene ◽  
Adp Glucose Pyrophosphorylase

scholarly journals Structure and expression analysis of genes encoding ADP-glucose pyrophosphorylase large subunit in wheat and its relatives

Genome ◽  
2016 ◽  
Vol 59 (7) ◽  
pp. 501-507 ◽  
Author(s):  
Xiao-Wei Zhang ◽  
Si-Yu Li ◽  
Ling-Ling Zhang ◽  
Qiang Yang ◽  
Qian-Tao Jiang ◽  
...  
Keyword(s):  
Large Subunit ◽  
Full Length ◽  
Starch Accumulation ◽  
Coding Region ◽  
D Genome ◽  
Reading Frame ◽  
B Genome ◽  
Genome Donor ◽  
Adp Glucose Pyrophosphorylase ◽  
Donor Species

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.

The role of the large subunit in redox regulation of the rice endosperm ADP-glucose pyrophosphorylase

FEBS Journal ◽  
2014 ◽  
Vol 281 (21) ◽  
pp. 4951-4963 ◽  
Author(s):  
Aytug Tuncel ◽  
Bilal Cakir ◽  
Seon-Kap Hwang ◽  
Thomas W. Okita
Keyword(s):  
Redox Regulation ◽  
Large Subunit ◽  
Rice Endosperm ◽  
Adp Glucose Pyrophosphorylase

Expression of a modified ADP-glucose pyrophosphorylase large subunit in wheat seeds stimulates photosynthesis and carbon metabolism

Planta ◽  
2006 ◽  
Vol 225 (4) ◽  
pp. 965-976 ◽  
Author(s):  
Eric D. Smidansky ◽  
Fletcher D. Meyer ◽  
Beth Blakeslee ◽  
Thaddeus E. Weglarz ◽  
Thomas W. Greene ◽  
...  
Keyword(s):  
Carbon Metabolism ◽  
Large Subunit ◽  
Adp Glucose Pyrophosphorylase ◽  
Wheat Seeds

Is There an Alternative Pathway for Starch Biosynthesis in Cereal Seeds?

1994 ◽  
Vol 49 (3-4) ◽  
pp. 215-219 ◽  
Author(s):  
Per Villand ◽  
Leszek A. Kleczkowski
Keyword(s):  
Direct Evidence ◽  
Alternative Pathway ◽  
Genetic Data ◽  
Starch Biosynthesis ◽  
Barley Seed ◽  
Barley Endosperm ◽  
Key Enzyme ◽  
Cereal Seed ◽  
Adp Glucose Pyrophosphorylase ◽  
Glucose Carrier

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

A mutant of rice lacking the leaf large subunit of ADP-glucose pyrophosphorylase has drastically reduced leaf starch content but grows normally

2007 ◽  
Vol 34 (6) ◽  
pp. 480 ◽  
Author(s):  
Sandrine Rösti ◽  
Brendan Fahy ◽  
Kay Denyer
Keyword(s):  
Environmental Conditions ◽  
No Reduction ◽  
Starch Content ◽  
Large Subunit ◽  
Starch Synthesis ◽  
Small Subunit ◽  
Wild Type ◽  
Gene Encoding ◽  
Subunit Protein ◽  
Adp Glucose Pyrophosphorylase

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.

Cloning and expression analysis of cDNAs encoding ADP-glucose pyrophosphorylase large and small subunits from hulless barley (Hordeum vulgare L. var. nudum)

2018 ◽  
Vol 73 (5-6) ◽  
pp. 191-197 ◽  
Author(s):  
Dongmei Li ◽  
Zhimin Yang ◽  
Xinchun Liu ◽  
Zhen Song ◽  
Zongyun Feng ◽  
...  
Keyword(s):  
Accumulation Rate ◽  
Large Subunit ◽  
Starch Synthesis ◽  
Small Subunit ◽  
Cloning And Expression ◽  
Starch Accumulation ◽  
Hordeum Vulgare L ◽  
Hulless Barley ◽  
Expression Levels ◽  
Adp Glucose Pyrophosphorylase

Abstract As an important plateau cereal crop, hulless barley is the principal food for the Tibetan people in China. ADP-glucose pyrophosphorylase (AGPase) is considered as the key enzyme for starch biosynthesis in plants. In this study, cDNAs encoding the small subunit (SSU I) and large subunit (LSU I) of AGPase were isolated from hulless barley. The results showed that SSU I and LSU I were 1438 and 1786 bp in length with a complete open reading frame (ORF) of 1419 and 1572 bp. The ORF-encoded polypeptides of 472 and 523 amino acids were having calculated molecular masses of 52.01 and 58.23 kDa, and the pI values were 5.59 and 6.30. In addition, phylogenetic analysis showed that SSU I and LSU I had the same phylogenetic trends with some species. Furthermore, expression levels in different growth periods and tissues of two hulless barley varieties were analyzed by quantitative reverse transcription-polymerase chain reaction. Gene expression levels of SSU I and LSU I were consistent with the total starch accumulation rate in endosperm. In conclusion, our data confirmed that SSU I and LSU I played an important role in hulless barley starch synthesis.

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