An amino-terminal deletion of rice phytochrome A results in a dominant negative suppression of tobacco phytochrome A activity in transgenic tobacco seedlings

Planta ◽  
1995 ◽  
Vol 197 (1) ◽  
Author(s):  
Karlheinz Emmler ◽  
J�rg Stockhaus ◽  
Nam-Hai Chua ◽  
Eberhard Sch�fer
Keyword(s):  
Transgenic Tobacco ◽  
Dominant Negative ◽  
Terminal Deletion ◽  
Phytochrome A ◽  
Amino Terminal ◽  
Tobacco Seedlings

Effects of truncated neurofilament proteins on the endogenous intermediate filaments in transfected fibroblasts

1991 ◽  
Vol 99 (2) ◽  
pp. 335-350 ◽  
Author(s):  
S.S. Chin ◽  
P. Macioce ◽  
R.K. Liem
Keyword(s):  
Intermediate Filament ◽  
Dominant Negative ◽  
Deletion Mutants ◽  
Tail Domain ◽  
Cultured Fibroblasts ◽  
Mutant Proteins ◽  
Amino Terminal ◽  
Novel Approach ◽  
Carboxyl Terminal

The expression and assembly characteristics of carboxyl- and amino-terminal deletion mutants of rat neurofilament low Mr (NF-L) and neurofilament middle Mr (NF-M) proteins were examined by transient transfection of cultured fibroblasts. Deletion of the carboxyl-terminal tail domain of either protein indicated that this region was not absolutely essential for co-assembly into the endogenous vimentin cytoskeleton. However, deletion into the alpha-helical rod domain resulted in an inability of the mutant proteins to co-assemble with vimentin into filamentous structures. Instead, the mutant proteins appeared to be assembled into unusual tubular-vesicular structures. Additionally, these latter deletions appeared to act as dominant negative mutants which induced the collapse of the endogenous vimentin cytoskeleton as well as the constitutively expressed NF-H and NF-M cytoskeletons in stably transfected cell lines. Thus, an intact alpha-helical rod domain was essential for normal IF co-assembly whereas carboxyl-terminal deletions into this region resulted in dramatic alterations of the existing type III and IV intermediate filament cytoskeletons in vivo. Deletions from the amino-terminal end into the alpha-helical rod region gave different results. With these deletions, the transfected protein was not co-assembled into filaments and the endogenous vimentin IF network was not disrupted, indicating that these deletion mutants are recessive. The dominant negative mutants may provide a novel approach to studying intermediate filament function within living cells.

Leaf-specific overexpression of plastidic glutamine synthetase stimulates the growth of transgenic tobacco seedlings

Planta ◽  
2000 ◽  
Vol 210 (2) ◽  
pp. 252-260 ◽  
Author(s):  
Andrea Migge ◽  
Elisa Carrayol ◽  
Bertrand Hirel ◽  
Thomas W. Becker
Keyword(s):  
Glutamine Synthetase ◽  
Transgenic Tobacco ◽  
Tobacco Seedlings

MdVHA-A encodes an apple subunit A of vacuolar H+-ATPase and enhances drought tolerance in transgenic tobacco seedlings

2013 ◽  
Vol 170 (6) ◽  
pp. 601-609 ◽  
Author(s):  
Qing-Long Dong ◽  
Chun-Rong Wang ◽  
Dan-Dan Liu ◽  
Da-Gang Hu ◽  
Mou-Jing Fang ◽  
...  
Keyword(s):  
Drought Tolerance ◽  
Transgenic Tobacco ◽  
Subunit A ◽  
Tobacco Seedlings

scholarly journals ACK Family Tyrosine Kinase Activity Is a Component of Dcdc42 Signaling during Dorsal Closure in Drosophila melanogaster

2002 ◽  
Vol 22 (11) ◽  
pp. 3685-3697 ◽  
Author(s):  
Kai Ping Sem ◽  
Baharak Zahedi ◽  
Ivan Tan ◽  
Maria Deak ◽  
Louis Lim ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Tyrosine Kinase ◽  
Kinase Activity ◽  
Leading Edge ◽  
Small Gtpase ◽  
Dominant Negative ◽  
Binding Motif ◽  
Dorsal Closure ◽  
Tyrosine Kinase Activity ◽  
Amino Terminal

ABSTRACT We have characterized Drosophila melanogaster ACK (DACK), one of two members of the ACK family of nonreceptor tyrosine kinases in Drosophila. The ACKs are likely effectors for the small GTPase Cdc42, but signaling by these proteins remains poorly defined. ACK family tyrosine kinase activity functions downstream of Drosophila Cdc42 during dorsal closure of the embryo, as overexpression of DACK can rescue the dorsal closure defects caused by dominant-negative Dcdc42. Similar to known participants in dorsal closure, DACK is enriched in the leading edge cells of the advancing epidermis, but it does not signal through activation of the Jun amino-terminal kinase cascade operating in these cells. Transcription of DACK is responsive to changes in Dcdc42 signaling specifically at the leading edge and in the amnioserosa, two tissues involved in dorsal closure. Unlike other members of the ACK family, DACK does not contain a conserved Cdc42-binding motif, and transcriptional regulation may be one route by which Dcdc42 can affect DACK function. Expression of wild-type and kinase-dead DACK transgenes in embryos, and in the developing wing and eye, reveals that ACK family tyrosine kinase activity is involved in a range of developmental events similar to that of Dcdc42.

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