Characterization of cDNA clones for rye endosperm β-amylase and analysis of β-amylase deficiency in rye mutant lines

1991 ◽  
Vol 83 (2) ◽  
pp. 257-263 ◽  
Author(s):  
T. Rorat ◽  
J. Sadowski ◽  
F. Grellet ◽  
J. Daussant ◽  
M. Delseny
Keyword(s):  
HortScience ◽  
2006 ◽  
Vol 41 (4) ◽  
pp. 1079B-1079
Author(s):  
Leslie Heffron ◽  
Emily Jordan ◽  
Jackie Nugent ◽  
Schuyler Korban

Sixteen putative ethylene mutant Antirrhinum majus (snapdragon) lines, derived from 1-aminocyclopropane-1-carboxylic acid (ACC) screening, were crossed in a full diallel that included the wild-type line to determine allelism/complementation groups. Seeds from these crosses were screened on a tissue culture medium containing 5 μM ACC to elucidate the response to exogenous ethylene treatment. Additionally, five of the mutant lines along with an inbred control, from which the mutants were derived, were analyzed using RT-PCR to determine regulation of gene expression in vegetative (roots, shoots, leaves, and sepals) and floral (six stages of flowering, from green bud to post-pollination) tissues using six different ACC synthase (ACS) cDNA clones and two different ethylene receptor (ETR) cDNA clones, all derived from Antirrhinum majus, as probes. Differential regulation of gene expression for ACS and ETR were observed in some tissues and at different stages of floral development.


1988 ◽  
Vol 263 (27) ◽  
pp. 13930-13936
Author(s):  
M Kurabayashi ◽  
I Komuro ◽  
H Tsuchimochi ◽  
F Takaku ◽  
Y Yazaki

1993 ◽  
Vol 23 (2) ◽  
pp. 365-376 ◽  
Author(s):  
Els J. M. Van Damme ◽  
Koen Smeets ◽  
Iris Engelborghs ◽  
Helen Aelbers ◽  
Jan Balzarini ◽  
...  
Keyword(s):  

1998 ◽  
Vol 36 (9) ◽  
pp. 647-656 ◽  
Author(s):  
Chye-Fong Liew ◽  
Chong-Jin Goh ◽  
Chiang-Shiong Loh ◽  
Saw-Hoon Lim

1991 ◽  
Vol 11 (10) ◽  
pp. 5113-5124 ◽  
Author(s):  
H Wu ◽  
A B Reynolds ◽  
S B Kanner ◽  
R R Vines ◽  
J T Parsons

Transformation of cells by the src oncogene results in elevated tyrosine phosphorylation of two related proteins, p80 and p85 (p80/85). Immunostaining with specific monoclonal antibodies revealed a striking change of subcellular localization of p80/85 in src-transformed cells. p80/85 colocalizes with F-actin in peripheral extensions of normal cells and rosettes (podosomes) of src-transformed cells. Sequence analysis of cDNA clones encoding p80/85 revealed an amino-terminal domain composed of six copies of a direct tandem repeat, each repeat containing 37 amino acids, a carboxyl-terminal SH3 domain, and an interdomain region composed of a highly charged acidic region and a region rich in proline, serine, and threonine. The multidomain structure of p80/85 and its colocalization with F-actin in normal and src-transformed cells suggest that these proteins may associate with components of the cytoskeleton and contribute to organization of cell structure.


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