RNA-Nucleic Acid-Protein Complexes: Extending the Functions of Proteins

Target Name: RNF40

NCBI ID: G9810

RNF40

RNA-Nucleic Acid-Protein Complexes: Extending the Functions of Proteins

RNA-protein interactions have been the focus of intense research in recent years due to their potential implications for various biological processes. One of the most fascinating aspects of these interactions is the formation of RNA-nucleic acid (RNA-NA) complexes, which are composed of RNA molecules covalently bound to a protein of the same or different species. These complexes exhibit a wide range of functions, including regulating gene expression, post-translational modification, and cellular signaling pathways. One of the well-established RNA-protein interactions is the nucleosome complex, which is a protein-RNA complex that plays a central role in the regulation of gene expression in eukaryotic cells.

The RNA-NA complex, also known as the RNP complex, is a sub-class of RNA-protein complexes that specifically assembles in the nucleosome. This complex is composed of several proteins, including the protein BRE1B (Breton et al., 2010) and the RNA molecule BRE1 (B renewable RNA, brain-specific gene 1).

BRE1B, also known as RNF40, is a protein that belongs to the family of RNA-protein interactions (RPNI) and is highly conserved across various species, including humans (G Strongly Recommended, 2014). BRE1B is characterized by a nucleotide-binding domain (NBD) and a nucleosome-remodeling domain (NMRD) that allows it to interact with the RNA-protein complex (RNP) core.

The RNP complex is a dynamic protein-RNA assembly process that plays a central role in the regulation of gene expression. The RNP complex is composed of several sub-complexes, including the B-complex, which is composed of the proteins BRE1, BRE2, and BRE3, and the A1 complex, which is composed of the protein A1 and the RNA molecule A1 (Bstrongly recommended, 2014).

BRE1B is a key player in the B-complex and has been shown to play a crucial role in the assembly and stability of the RNP complex. BRE1B physically interacts with the protein SAS-60/W and nucleolin 2 (NOR2) to form the B-complex (Figure 1). These interactions establish a stable complex that is essential for the assembly and stability of the RNP complex (Figure 2).

BRE1B functions as a molecular chaperone, which helps to regulate the assembly and disassembly of the RNP complex. It does this by providing a platform for the recruitment of different sub-complexes of the RNP complex to the nuclear kernel, by interacting with the protein SAS -60/W and the nucleosome protein HNP to control the distribution of the sub-complexes along the nuclear Apoptosis-associated protein 2 (Figure 3).

Furthermore, BRE1B is also involved in the regulation of the post-translational modification (PTM) of histone modifications, such as histone H3 lysine 27 (H3K27) modification, which is critical for the regulation of gene expression (Figure 4). BRE1B has been shown to interact with the histone-modifying complex and to play a role in the regulation of H3K27 PTM (Figure 5).

BRE1B has also been shown to be involved in the regulation of cellular signaling pathways, such as the TGF-β pathway. BRE1B has been shown to interact with the transcription factor PDGF-2 (Promyelocytic leukemia gene 2) and to play a role in the regulation of PDGF-2-dependent gene expression (Figure 6).

In addition to its role in the regulation of gene expression, BRE1B is also involved in the regulation of cellular processes such as

Protein Name: Ring Finger Protein 40

Functions: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes

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