Molecular characterization of the diurnal/circadian expression of the chlorophyll a/b-binding proteins in leaves of tomato and other dicotyledonous and monocotyledonous plant species

Planta ◽  
1989 ◽  
Vol 180 (1) ◽  
pp. 5-15 ◽  
Author(s):  
Hartmut Meyer ◽  
Ute Thienel ◽  
Birgit Piechulla
Keyword(s):  
Molecular Characterization ◽  
Chlorophyll A ◽  
Plant Species ◽  
Binding Proteins ◽  
Monocotyledonous Plant ◽  
Circadian Expression

Molecular characterization of tobacco cDNAs encoding two small GTP-binding proteins

1992 ◽  
Vol 19 (5) ◽  
pp. 847-857 ◽  
Author(s):  
Geza Dallmann ◽  
Liliane Sticher ◽  
Christopher Marshallsay ◽  
Ferenc Nagy
Keyword(s):  
Molecular Characterization ◽  
Binding Proteins ◽  
Gtp Binding Proteins ◽  
Gtp Binding

Molecular characterization of fibronectin binding proteins in bacteria

1993 ◽  
Vol 18 (3) ◽  
pp. 213-226 ◽  
Author(s):  
Arne N. Olsén ◽  
Emauel Hanski ◽  
Staffan Normakr ◽  
Michael G. Caparon
Keyword(s):  
Molecular Characterization ◽  
Binding Proteins ◽  
Fibronectin Binding

Molecular Characterization of High Plant Species Using PCR with Primers Designed from Consensus Branch Point Signal Sequences

2011 ◽  
Vol 49 (5-6) ◽  
pp. 352-363 ◽  
Author(s):  
Faqian Xiong ◽  
Jing Jiang ◽  
Zhuqiang Han ◽  
Ruichun Zhong ◽  
Liangqiong He ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Plant Species ◽  
Branch Point ◽  
Signal Sequences

scholarly journals Molecular characterization of 5-chlorophyll a/b-binding protein genes from Panax ginseng Meyer and their expression analysis during abiotic stresses

2016 ◽  
Vol 54 (3) ◽  
pp. 446-458 ◽  
Author(s):  
J. Silva ◽  
Y. J. Kim ◽  
J. Sukweenadhi ◽  
S. Rahimi ◽  
W. S. Kwon ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Chlorophyll A ◽  
Panax Ginseng ◽  
Expression Analysis ◽  
Abiotic Stresses ◽  
Binding Protein

scholarly journals Identification and molecular characterization of E-MAP-115, a novel microtubule-associated protein predominantly expressed in epithelial cells.

1993 ◽  
Vol 123 (2) ◽  
pp. 357-371 ◽  
Author(s):  
D Masson ◽  
T E Kreis
Keyword(s):  
Epithelial Cells ◽  
Molecular Characterization ◽  
Hela Cells ◽  
Binding Proteins ◽  
Cdna Expression Library ◽  
Expression Library ◽  
Microtubule Binding ◽  
Terminal Domain

A novel microtubule-associated protein (MAP) of M(r) 115,000 has been identified by screening of a HeLa cell cDNA expression library with an anti-serum raised against microtubule-binding proteins from HeLa cells. Monoclonal and affinity-purified polyclonal antibodies were generated for the further characterization of this MAP. It is different from the microtubule-binding proteins of similar molecular weights, characterized so far, by its nucleotide-insensitive binding to microtubules and different sedimentation behavior. Since it is predominantly expressed in cells of epithelial origin (Caco-2, HeLa, MDCK), and rare (human skin, A72) or not detectable (Vero) in fibroblastic cells, we name it E-MAP-115 (epithelial MAP of 115 kD). In HeLa cells, E-MAP-115 is preferentially associated with subdomains or subsets of perinuclear microtubules. In Caco-2 cells, labeling for E-MAP-115 increases when they polarize and form blisters. The molecular characterization of E-MAP-115 reveals that it is a novel protein with no significant homologies to other known proteins. The secondary structure predicted from its sequence indicates two domains connected by a putative hinge region rich in proline and alanine (PAPA region). E-MAP-115 has two highly charged regions with predicted alpha-helical structure, one basic with a pI of 10.9 in the NH2-terminal domain and one neutral with a pI of 7.6 immediately following the PAPA region in the acidic COOH-terminal half of the molecule. A novel microtubule-binding site has been localized to the basic alpha-helical region in the NH2-terminal domain using in vitro microtubule-binding assays and expression of mutant polypeptides in vivo. Overexpression of this domain of E-MAP-115 by transfection of fibroblasts lacking significant levels of this protein with its cDNA renders microtubules stable to nocodazole. We conclude that E-MAP-115 is a microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells.

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