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The hnRNPs are RNA binding proteins that form a complex with heterogeneous nuclear RNA [8].
Regulation of gene expression involves complex dynamics employing sequence-specific DNA binding proteins that form the transcriptional regulatory network (Babu et al., 2004; Jothi et al., 2009; Luscombe et al., 2004).
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The S100 protein family consists of small (10 12 kDa), acidic calcium-binding proteins that form noncovalent homo- or heterodimers.
The septins are conserved GTP-binding proteins that form filaments during cell divisions or cytokinesis [ 54, 55].
The reduced overall surface area of a short oligonucleotide also results in a lower local concentration of condensing bodies; for DNA, these may be ions or DNA-binding proteins that form a local region of high concentration simply by their affinity for DNA (and in the case of proteins, irrespective of sequence).
In addition to a predicted interaction with 14-3-3 14-3-3 14-3-3egulate chromatin, fly Akirin (as Bhringi) was shown to bind Baproteins], a DNA binding protoin that foregulate of the SWI/SNF-like chromatin remodelling complex [ 48] which is highly conserved in eukaryotes.
Tsunagi is a RNA binding protein that forms a complex with another protein called Mago Nashi.
The sugABC operon, an ABC transporter, is best characterized in M. tuberculosis and is composed of a periplasmic sugar binding protein that forms a lipid anchor (LpqY), a transmembrane protein (a heterodimer of sugA and sugB) and a terminal ATP-binding cytoplasmic protein (sugC).
HCV core protein, the first structural protein encoded by the HCV open reading frame, is a highly conserved RNA-binding protein that forms the viral nucleocapsid [3].
TDP-43 is an RNA-binding protein that forms heterogeneous nuclear ribonucleoprotein complexes (hnRNP) which function in RNA processing activities of several cellular functions, including transcription, RNA splicing and microRNA processing [ 16, 17, 118].
Moreover, the gene sraP, which encodes a platelet-binding protein that forms a fimbria-like structure involved in adhesion, is normally organized in an operon with genes encoding a specific secretion (sec) system (SecA2, SecY2) and a glycosyltransferase, which are responsible for the translocation and glycosylation, respectively, of the SraP protein [ 63].
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