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Isolation of a Calmodulin-binding Transcription Factor from Rice (Oryza sativa L.)
Choi, Man-Soo,Kim, Min-Chul,Yoo, Jae-Hyuk,Moon, Byeong-Cheol,Koo, Sung-Cheo,Park, Byung-Ouk,Lee, Ju-Huck,Koo, Yoon-Duck,Han, Hay-Ju,Lee, Sang-Yeol,Chung, Woo-Sik,Lim, Chae-Oh,,Cho, Moo-Je Plant molecular biology and biotechnology research 2005 Plant molecular biology and biotechnology research Vol.2005 No.
Calmodulin (CaM) regulates diverse cellular functions by modulating the activities of a variety of enzymes and proteins. However, direct modulation of transcription factors by CaM has been poorly understood. In this study, we isolated a putative transcription factor by screening a rice cDNA expression library by using CaM:horseradish peroxidase as a probe. This factor, which we have designated OsCBT (Oryza sativa CaM-binding transcription factor), has structural features similar to Arabidopsis AtSRs/AtCAMTAs and encodes a 103-kDa protein because it contains a CG-1 homology DNA-binding domain, three ankyrin repeats, a putative transcriptional activation domain, and five putative CaM-binding motifs. By using a gel overlay assay, gel mobility shift assays, and site-directed mutagenesis, we showed that OsCBT has two different types of functional CaM-binding domains, an IQ motif, and a Ca^(2+)-dependent motif. To determine the DNA binding specificity of OsCBT, we employed a random binding site selection method. This analysis showed that OsCBT preferentially binds to the sequence 5'-TWCG(C/T)GTKKKKTKCG-3' (W and K represent A or C and T or G, respectively). OsCBT was able to bind this sequence and activate β-glucuronidase reporter gene expression driven by a minimal promoter containing tandem repeats of these sequences in Arabidopsis leaf protoplasts. Green fluorescent protein fusions of two putative nuclear localization signals of OsCBT, a bipartite and a SV40 type, were predominantly localized in the nucleus. Most interestingly, the transcriptional activation mediated by OsCBT was inhibited by co-transfection with a CaM gene. Taken together, our results suggest that OsCBT is a transcription activator modulated by CaM.
WRKY group IId transcription factors interact with calmodulin
Park, Chan Young,Lee, Ju Huck,Yoo, Jae Hyuk,Moon, Byeong Cheol,Choi, Man Soo,Kang, Yun Hwan,Lee, Sang Min,Kim, Ho Soo,Kang, Kyu Young,Chung, Woo Sik,Lim, Chae Oh,Cho, Moo Je Elsevier 2005 FEBS letters Vol.579 No.6
<P><B>Abstract</B></P><P>Calmodulin (CaM) is a ubiquitous Ca<SUP>2+</SUP>-binding protein known to regulate diverse cellular functions by modulating the activity of various target proteins. We isolated a cDNA encoding AtWRKY7, a novel CaM-binding transcription factor, from an <I>Arabidopsis</I> expression library with horseradish peroxidase-conjugated CaM. CaM binds specifically to the Ca<SUP>2+</SUP>-dependent CaM-binding domain (CaMBD) of AtWRKY7, as shown by site-directed mutagenesis, a gel mobility shift assay, a split-ubiquitin assay, and a competition assay using a Ca<SUP>2+</SUP>/CaM-dependent enzyme. Furthermore, we show that the CaMBD of AtWRKY7 is a conserved structural motif (C-motif) found in group IId of the WRKY protein family.</P>
Induction of anti-tumor immunity by vaccination with E7 of HPV16 and IL-12
송민종 ( Min Jong Song ),( Ju Huck Choi ),( Byung Hun Kim ),( Su Mi Bae ),( Hae Nam Kim ),( Eun Kyung Park ),( Jun Mo Lee ),( Sung Eun Namkoong ),( Kim Dou Kang ),( Chong Kook Kim ),( Jin Hyun Sun ),( Ju 대한산부인과학회 2004 대한산부인과학회 학술대회 Vol.90 No.-
WRKY group Ⅱd transcription factors interact with calmodulin
Park, Chan-Young,Lee, Ju-Huck,Yoo, Jae-Hyuk,Moon, Byeong-Cheol,Choi, Man-Soo,Kang, Yun-Hwan,Lee, Sang-Min,Kim, Ho-Soo,Kang, Kyu-Young,Chung, Woo-Sik,,Lim, Chae-Oh,Cho, Moo-Je Plant molecular biology and biotechnology research 2005 Plant molecular biology and biotechnology research Vol.2005 No.
Calmodulin (CaM) is a ubiquitous Ca^(2+)-binding protein known to regulate diverse cellular functions by modulating the activity of various target proteins. We isolated a cDNA encoding AtWRKY7, a novel CaM-binding transcription factor, from an Arabidopsis expression library with horseradish peroxidase-conjugated CaM. CaM binds specifically to the Ca^(2+)-dependent CaM-binding domain (CaMBD) of AtWRKY7, as shown by site-directed mutagenesis, a gel mobility shift assay, a split-ubiquitin assay, and a competition assay using a Ca^(2+)/CaM-dependent enzyme. Furthermore, we show that the CaMBD of AtWRKY7 is a conserved structural motif (C-motif) found in group Ⅱd of the WRKY protein family. ⓒ 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Park, Chan-Young,Heo, Won-Do,Yoo, Jae-Hyuk,Lee, Ju-Huck,Kim, Min-Chul,Chun, Hyun-Jin,Moon, Byeong-Cheol,Kim, Ihn-Hyeong,Park, Hyeong-Cheol,Choi, Man-Soo,Ok, Hyun-Mi,Cheong, Mi-Sun,Lee, Sang-Min,Kim, H Plant molecular biology and biotechnology research 2004 Plant molecular biology and biotechnology research Vol.2004 No.-
Plants produce numerous calmodulin isoforms that exhibit differential gene expression patterns and sense different Ca^(2+)signals. This diversity results in different physiological responses to particular stimuli. GmCaM-4 and -5 are two divergent calmodulin isoforms from the soybean (Glycine max) that have been reported to be involved in plant disease resistance. However, little is known about the pathway by which these specific isoforms transduce the defense signal and up-regulate pathogenesis-related (PR) genes. Here we report that overexpression of GmCaM-4/-5 induces constitutive PR gene expression and enhances disease resistance in wild-type Arabidopsis, but not in the nim1 mutant of Arabidopsis. GmCaM-4/-5 also appear to activate trans-acting elements that bind to cis-acting elements in the Arabidopsis PR-1 promoter. Thus up-regulation of PR genes by these GmCaM isoforms is dependent on NIM1 (Non immunity 1) and unknown transcription factors.
Mediterraneibacter butyricigenes sp. nov., a butyrate-producing bacterium isolated from human faeces
Kim, Ji-Sun,Lee, Keun Chul,Suh, Min Kuk,Han, Kook-Il,Eom, Mi Kyung,Lee, Ju Huck,Park, Seung-Hwan,Kang, Se Won,Park, Jam-Eon,Oh, Byeong Seob,Yu, Seung Yeob,Choi, Seung-Hyeon,Lee, Dong Ho,Yoon, Hyuk,Kim MICROBIOLOGICAL SOCIETY OF KOREA 2019 JOURNAL OF MICROBIOLOGY -SEOUL- Vol.57 No.1