scholarly journals Expression, purification, and characterization of an intrinsically disordered Late Embryogenesis Abundant (LEA) protein from Artemia franciscana utilizing Escherichia coli and Nicotiana tabacum

2017 ◽  
Vol 31 (S1) ◽  
Author(s):  
Md Fazlul Karim ◽  
Yordan S. Yordanov ◽  
Michael A. Menze
Keyword(s):  
Escherichia Coli ◽  
Nicotiana Tabacum ◽  
Late Embryogenesis Abundant ◽  
Artemia Franciscana ◽  
Lea Protein ◽  
Purification And Characterization ◽  
Intrinsically Disordered ◽  
Late Embryogenesis

Characterization of a group 1 late embryogenesis abundant protein in encysted embryos of the brine shrimp Artemia franciscana

2009 ◽  
Vol 87 (2) ◽  
pp. 415-430 ◽  
Author(s):  
Michelle A. Sharon ◽  
Anna Kozarova ◽  
James S. Clegg ◽  
Panayiotis O. Vacratsis ◽  
Alden H. Warner
Keyword(s):  
Amino Acids ◽  
Brine Shrimp ◽  
Animal Species ◽  
Late Embryogenesis Abundant ◽  
Lea Proteins ◽  
Lea Protein ◽  
Late Embryogenesis ◽  
Its Gene ◽  
Group 1

Late embryogenesis abundant (LEA) proteins are hydrophilic molecules that are believed to function in desiccation and low-temperature tolerance in some plants and plant propagules, certain prokaryotes, and several animal species. The brine shrimp Artemia franciscana can produce encysted embryos (cysts) that enter diapause and are resistant to severe desiccation. This ability is based on biochemical adaptations, one of which appears to be the accumulation of the LEA protein that is the focus of this study. The studies described herein characterize a 21 kDa protein in encysted Artemia embryos as a group 1 LEA protein. The amino acid sequence of this protein and its gene have been determined and entered into the NCBI database (no. EF656614). The LEA protein consists of 182 amino acids and it is extremely hydrophilic, with glycine (23%), glutamine (17%), and glutamic acid (12.6%) being the most abundant amino acids. This protein also consists of 8 tandem repeats of a 20 amino acid sequence, which is characteristic of group 1 LEA proteins from non-animal species. The LEA protein and its gene are expressed only in encysted embryos and not in larvae or adults. Evidence is presented to show that the LEA protein functions in the prevention of drying-induced protein aggregation, which supports its functional role in desiccation tolerance. This report describes, for the first time, the purification and characterization of a group 1 LEA protein from an animal species.

Purification and characterization of Escherichia coli formamidopyrimidine-DNA glycosylase that excises damaged 7-methylguanine from deoxyribonucleic acid

Biochemistry ◽  
1981 ◽  
Vol 20 (18) ◽  
pp. 5201-5207 ◽  
Author(s):  
Christopher J. Chetsanga ◽  
Marie Lozon ◽  
Christopher Makaroff ◽  
Laura Savage
Keyword(s):  
Escherichia Coli ◽  
Deoxyribonucleic Acid ◽  
Dna Glycosylase ◽  
Purification And Characterization

scholarly journals The Purification and Characterization of Escherichia coli Enolase

1971 ◽  
Vol 246 (22) ◽  
pp. 6797-6802
Author(s):  
Thomas G. Spring ◽  
Finn Wold
Keyword(s):  
Escherichia Coli ◽  
Purification And Characterization

scholarly journals Purification and characterization of Escherichia coli RNase T.

1985 ◽  
Vol 260 (11) ◽  
pp. 7067-7071
Author(s):  
M P Deutscher ◽  
C W Marlor
Keyword(s):  
Escherichia Coli ◽  
Purification And Characterization
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