Molecular cloning of an actinobacterial-type ClpS gene from Celosia cristata expression library

التفاصيل البيبلوغرافية
العنوان: Molecular cloning of an actinobacterial-type ClpS gene from Celosia cristata expression library
المؤلفون: B. BaghbanKohnehrouz, A. Gholizadeh, M. H. Faizi, H. C. Kapoor
المصدر: Russian Journal of Plant Physiology. 55:521-529
بيانات النشر: Pleiades Publishing Ltd, 2008.
سنة النشر: 2008
مصطلحات موضوعية: Genetics, biology, Celosia cristata, Chaperone (protein), Complementary DNA, Protein domain, biology.protein, Coding region, Plant Science, Molecular cloning, biology.organism_classification, Gene, Peptide sequence
الوصف: In proteobacterial cytosol, ClpS protein is known as a molecular adaptor for substrate selectivity and proteolytic activity of the ATP-dependent chaperone-protease complex, ClpAP. ClpA-related ClpS is a small protein usually encoded immediately upstream of ClpA in the genome of proteobacteria. Recent bioinformatics analysis has revealed the presence of cyanobacterial-type ClpS or ClpC-related ClpS in organisms lacking ClpA, including all the plant species sequenced to date. Here we report the identification of an actinobacterial homologue of the ClpS (possibly Clp-related) gene from a plant system. A cDNA, spanning 566 bp with a complete coding region corresponding to 132 amino acids, was isolated from a Celosia cristata expression library constructed on a λ TriplEX2 vector. This cDNA product was considered to be an ATP-dependent Clp protease adaptor and was designated as Celosia actinobacterial-type ClpS, since it contains a highly conserved domain belonging to the ClpS family of proteins from actinobacteria. Celosia ClpS is about 80% identical to actinobacterial ClpS proteins in its overall deduced amino acid sequence. Based on this finding, we may define a novel target of ATP-dependent Clp complex in a plant system or speculate the presence of a second type of molecular chaperone besides ClpC in plants, as predicted for actinobacteria.
تدمد: 1608-3407
1021-4437
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::2243a21ba9e04e42b66d88415b1e89b6Test
https://doi.org/10.1134/s1021443708040146Test
حقوق: CLOSED
رقم الانضمام: edsair.doi...........2243a21ba9e04e42b66d88415b1e89b6
قاعدة البيانات: OpenAIRE