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PUF proteins, named for Drosophila Pumilio (PUM) and Caenorhabditis elegans fem-3-binding factor (FBF), recognize specific sequences in the mRNAs they bind and control. RNA binding by classical PUF proteins is mediated by a characteristic PUM homology domain (PUM-HD). The Puf1 and Puf2 proteins possess a distinct architecture and comprise a highly conserved subfamily among fungal species. Puf1/Puf2 proteins contain two types of RNA-binding domain: a divergent PUM-HD and an RNA recognition motif (RRM). They recognize RNAs containing UAAU motifs, often in clusters. Here, we report a crystal structure of the PUM-HD of a fungal Puf1 in complex with a dual UAAU motif RNA. Each of the two UAAU tetranucleotides are bound by a Puf1 PUM-HD forming a 2:1 protein-to-RNA complex. We also determined crystal structures of the Puf1 RRM domain that identified a dimerization interface. The PUM-HD and RRM domains act in concert to determine RNA-binding specificity: the PUM-HD dictates binding to UAAU, and dimerization of the RRM domain favors binding to dual UAAU motifs rather than a single UAAU. Cooperative action of the RRM and PUM-HD identifies a new mechanism by which multiple RNA-binding modules in a single protein collaborate to create a unique RNA-binding specificity.
This article was published in the following journal.
Name: Nucleic acids research
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Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.
A class of proteins related in structure and function to TATA-BOX BINDING PROTEIN that can take the place of TATA-BOX BINDING PROTEIN in the transcription initiation complex. They are found in most multicellular organisms and may be involved in tissue-specific promoter regulation. They bind to DNA and interact with TATA-BINDING PROTEIN ASSOCIATED FACTORS, however they may lack specificity for the TATA-BOX.
A poly(A) binding protein that is involved in promoting the extension of the poly A tails of MRNA. The protein requires a minimum of ten ADENOSINE nucleotides in order for binding to mRNA. Once bound it works in conjunction with CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR to stimulate the rate of poly A synthesis by POLY A POLYMERASE. Once poly-A tails reach around 250 nucleotides in length poly(A) binding protein II no longer stimulates POLYADENYLATION. Mutations within a GCG repeat region in the gene for poly(A) binding protein II have been shown to cause the disease MUSCULAR DYSTROPHY, OCULOPHARYNGEAL.
Protein modules that function in the targeting of proteins to CELL MEMBRANES. They consist of an eight-stranded anti-parallel beta-sandwich composed of a pair of four-stranded beta-sheets. This structural unit forms a pocket on the membrane-interacting face of the protein and co-ordinates the binding of 2 to 3 calcium ions; however, not all C2 domains bind calcium. Examples of C2 domain-containing proteins include PROTEIN KINASE C and PTEN PHOSPHOHYDROLASE.
Gram-negative bacterial secretion systems which translocate effectors in a single step across the inner and outer membranes. The one-step secretion is carried out by a channel that passes from the CYTOPLASM, through the inner membrane, PERIPLASMIC SPACE, and outer membrane, to the EXTRACELLULAR SPACE. The specificity of type I secretions systems are determined by the specificity of the three subcomponents forming the channel - an ATP transporter (ATP-BINDING CASSETTE TRANSPORTERS); a membrane fusion protein (MEMBRANE FUSION PROTEINS); and an outer membrane protein (BACTERIAL OUTER MEMBRANE PROTEINS.)
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Collaborations in biotechnology
Commercial and academic collaborations are used throughout the biotechnology and pharmaceutical sector to enhance research and product development. Collaborations can take the form of research and evaluation agreements, licensing, partnerships etc. ...