Nucleotide sequence of a gene encoding a 58.5-kilodalton barley dehydrin that lacks a serine tract.
نویسندگان
چکیده
Dehydrins, also known as the late embryogenesis abundant (LEA) D-11 family of proteins (Close et al., 1993, and refs. therein), generally accumulate in plants in response to water deficit, embryo desiccation, cold temperature, reduction in externa1 osmotic potential, or application of ABA. Over 40 examples of deduced amino acid sequences of higher plant dehydrins have been published to date, and there is immunological evidence of related proteins in organisms as distant from higher plants as cyanobacteria (Close and Lammers, 1993). Known members of this family of proteins are characterized by the presence of highly conserved repeating motifs including the Lys-rich 15amino acid consensus EKKGIMDKIKEKLPG, which is always located near the carboxy terminus (the lone exception being cotton LEA D-11). A related but slightly less conserved consensus sequence is usually repeated at least once and up to 10 additional times in published examples of plant dehydrins. Dehydrins can be divided into two main classes, those containing approximately nine consecutive Ser residues and those without this Ser tract. The Ser residues in this tract can be phosphorylated, and it has been proposed that phosphorylation of Ser's is related to the binding of nuclear localization signal peptides (Goday et al., 1994). Dehydrins have a nucleocytoplasmic location (Asghar et al., 1994; Goday et al., 1994). The majority of dehydrins identified to date fall into the class that contains the Ser tract, and the minority fall into the latter class, without the Ser tract. Those in the former class usually contain two or three Lys-rich consensus blocks. Dehydrins in the latter class usually contain six or more consensus blocks. There are exceptions to these generalizations, and each class can be subdivided further based on intervening amino acid sequences located between the consensus blocks. Examples of dehydrins that lack a Ser tract include spinach CAP85 (61.5 kD with 11 repeats) (Neven et al., 1993), wheat WCS120 (39.0 kD with 6 repeats) (Houde et al., 1992)' and wheat COR39 (39.1 kD
منابع مشابه
Nucleotide Sequence of Gene Encoding Capsid Protein VPI of Foot-and-Mouth Disease Virus / Type O1 Iran
متن کامل
Bioinformatic and empirical analysis of a gene encoding serine/threonine protein kinase regulated in response to chemical and biological fertilizers in two maize (Zea mays L.) cultivars
Molecular structure of a gene, ZmSTPK1, encoding a serine/threonine protein kinase in maize was analyzed by bioinformatic tool and its expression pattern was studied under chemical biological fertilizers. Bioinformatic analysis cleared that ZmSTPK1 is located on chromosome 10, from position 141015332 to 141017582. The full genomic sequence of the gene is 2251 bp in length and includes 2 exons. ...
متن کاملNucleotide sequence of cDNA encoding for preprochymosin in native goat (Capra hircus) from Iran
Prochymosin is one of the most important aspartic proteinases used as a milk-clotting enzyme in cheese production. In the present investigation we report sequence of cDNA encoding goat ( Capra hircus ) preprochymosin and compare its nucleotide and deduced amino acid sequences with sequences of other ruminants preprochymosin. As bovine prochymosin, the caprine prochymosin cDNA encodes 365 amino ...
متن کاملCloning and sequence analysis of a highly polymorphic Cryptosporidium parvum gene encoding a 60-kilodalton glycoprotein and characterization of its 15- and 45-kilodalton zoite surface antigen products.
The apicomplexan parasite Cryptosporidium parvum is a major cause of serious diarrheal disease in both humans and animals. No efficacious chemo- or immunotherapies have been identified for cryptosporidiosis, but certain antibodies directed against zoite surface antigens and/or proteins shed by gliding zoites have been shown to neutralize infectivity in vitro and/or to passively protect against,...
متن کاملThe Importance of Size and Disorder in the Cryoprotective Effects of Dehydrins1[C][W]
Dehydrins protect plant proteins and membranes from damage during drought and cold. Vitis riparia K2 is a 48-residue protein that can protect lactate dehydrogenase from freeze-thaw damage by preventing the aggregation and denaturation of the enzyme. To further elucidate its mechanism, we used a series of V. riparia K2 concatemers (K4, K6, K8, and K10) and natural dehydrins (V. riparia YSK2, 60 ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Plant physiology
دوره 107 1 شماره
صفحات -
تاریخ انتشار 1995