Regular ArticleExpression and cDNA Cloning of Human HMGI-C Phosphoprotein
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2004, Pathology Research and PracticeCitation Excerpt :High mobility group (HMG) proteins are heterogeneous non-histone DNA-binding factors that organize active chromatin [10,11,30]. HMGI-C is a member of the HMGI family of HMG proteins and consists of 109 amino acids residues [21]. The HMGI-C gene is located on chromosome 12 [14].
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2003, Methods in EnzymologyCitation Excerpt :For this purpose, we have found the pET bacterial expression vector systems, originally developed by Studier and colleagues18,19 and now commercially available from Novagen (Madison, WI), to be especially useful.8,20,21 By employing standard in vitro mutagenesis techniques and recombinant DNA procedures,22 full-length, mutant, or truncated forms of the cDNAs encoding either the HMGA1a, HMGA1b,23 or HMG224 proteins are subcloned into the appropriate pET expression vector, which is then transformed into the double lon⧸ompT protease mutant B strain of Escherichia coli BL21(DE3)pLysS.19 Alternatively, to overcome problems of codon bias and greatly increase the yield of recovered proteins, the cDNA-containing pET vectors can be transformed into the BL21-CodonPlus-RP strain of E. coli (Stratagene, La Jolla, CA), which has been genetically engineered to express tRNAs that recognize arginine (AGG⧸AGA) and proline (CCC) codons that are rarely used in bacteria but are common in transcripts encoding HMGA proteins.