Conservation of Matrix Attachment Region-Binding Filament-Like Protein 1 among Higher Plants1

AUTOR(ES)

Harder, Patricia A.

FONTE

American Society of Plant Physiologists

RESUMO

The interaction of chromatin with the nuclear matrix via matrix attachment regions (MARs) on the DNA is considered to be of fundamental importance for higher-order chromatin organization and the regulation of gene expression. We have previously isolated a novel nuclear matrix-localized protein (MFP1) from tomato (Lycopersicon esculentum) that preferentially binds to MAR DNA. Tomato MFP1 has a predicted filament-protein-like structure and is associated with the nuclear envelope via an N-terminal targeting domain. Based on the antigenic relationship, we report here that MFP1 is conserved in a large number of dicot and monocot species. Several cDNAs were cloned from tobacco (Nicotiana tabacum) and shown to correspond to two tobacco MFP1 genes. Comparison of the primary and predicted secondary structures of MFP1 from tomato, tobacco, and Arabidopsis indicates a high degree of conservation of the N-terminal targeting domain, the overall putative coiled-coil structure of the protein, and the C-terminal DNA-binding domain. In addition, we show that tobacco MFP1 is regulated in an organ-specific and developmental fashion, and that this regulation occurs at the level of transcription or RNA stability.

Documentos Relacionados

• MFP1, a novel plant filament-like protein with affinity for matrix attachment region DNA.
• The matrix attachment region-binding protein SATB1 participates in negative regulation of tissue-specific gene expression.
• Enzymatic Synthesis of Glutamine in Higher Plants1
• Enzymatic Synthesis of Gamma-Glutamyl-Cysteine in Higher Plants1
• Matrix attachment region binding protein MFP1 is localized in discrete domains at the nuclear envelope.