Grotewold Lab: Antje Feller

One of the main goals in the Grotewold lab is to understand the function of maize transcription factors and their role in combinatorial transcriptional control.

My research focuses on the maize bHLH transcription factor R and its function in transcriptional regulation and chromatin remodeling. R is an essential co-activator of the MYB-domain protein C1 in regulating the maize anthocyanin biosynthetic pathway. It enhances transcriptional activation by directly binding or by recruiting a second binding factor to the ARE (anthocyanin regulatory element), a cis regulatory element present in several anthocyanin biosynthetic genes.

In addition, R interacts with many proteins, therefore we hypothesize that R allows the formation of a complex on flavonoid gene promoters. The Myb-interacting region of R (amino acids 1-251) interacts with the MYB domain protein C1. The acidic domain (amino acids 252-415) interacts with the WD40 protein Pac1, which has been shown to be involved in flavonoid biosynthesis. In addition, we have recently shown that R contains an ACT-like dimerization domain (amino acids 525-610) at its C-terminal region. We found that homodimerization through the ACT-like domain is necessary for the regulatory function of R. Interestingly, many arabidopsis bHLH transcription factors contain an ACT-like domain in addition to the well conserved bHLH dimerization domain (amino acids 411-462). The bHLH domain is necessary for activation of endogenous genes but not transiently introduced genes in cultured maize Black Mexican Sweet cells, suggesting a role of the bHLH in chromatin remodeling.

In yeast two-hybrid screens I have identified two maize bHLH proteins which interact with the bHLH domain of R. Presently, I’m characterizing these two proteins and try to understand how they are contributing to R function. In addition, we identified a third protein which interacts with the bHLH domain of R. This R-interacting-factor 1 (RIF1) has an ENT domain and an AGENET domain and we have recently shown that this protein links transcriptional regulation and histone modification.



		Antje Feller Research Interests I’m a 4th year graduate student in the Molecular Cellular and Developmental Biology program in the Department of Plant, Cellular and Molecular Biology. One of the main goals in the Grotewold lab is to understand the function of maize transcription factors and their role in combinatorial transcriptional control. My research focuses on the maize bHLH transcription factor R and its function in transcriptional regulation and chromatin remodeling. R is an essential co-activator of the MYB-domain protein C1 in regulating the maize anthocyanin biosynthetic pathway. It enhances transcriptional activation by directly binding or by recruiting a second binding factor to the ARE (anthocyanin regulatory element), a cis regulatory element present in several anthocyanin biosynthetic genes. In addition, R interacts with many proteins, therefore we hypothesize that R allows the formation of a complex on flavonoid gene promoters. The Myb-interacting region of R (amino acids 1-251) interacts with the MYB domain protein C1. The acidic domain (amino acids 252-415) interacts with the WD40 protein Pac1, which has been shown to be involved in flavonoid biosynthesis. In addition, we have recently shown that R contains an ACT-like dimerization domain (amino acids 525-610) at its C-terminal region. We found that homodimerization through the ACT-like domain is necessary for the regulatory function of R. Interestingly, many arabidopsis bHLH transcription factors contain an ACT-like domain in addition to the well conserved bHLH dimerization domain (amino acids 411-462). The bHLH domain is necessary for activation of endogenous genes but not transiently introduced genes in cultured maize Black Mexican Sweet cells, suggesting a role of the bHLH in chromatin remodeling. In yeast two-hybrid screens I have identified two maize bHLH proteins which interact with the bHLH domain of R. Presently, I’m characterizing these two proteins and try to understand how they are contributing to R function. In addition, we identified a third protein which interacts with the bHLH domain of R. This R-interacting-factor 1 (RIF1) has an ENT domain and an AGENET domain and we have recently shown that this protein links transcriptional regulation and histone modification.

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