Secondary literature sources for FF
The following references were automatically generated.
- Zhang H et al.
- A novel C1q-domain-containing protein from Zhikong scallop Chlamys farreriwith lipopolysaccharide binding activity.
- Fish Shellfish Immunol. 2008; 25: 281-9
- Display abstract
The C1q-domain-containing (C1qDC) proteins are a family of proteinscharacterized by a globular C1q (gC1q) domain in their C-terminus. Theyare involved in various processes of vertebrates and supposed to be animportant pattern recognition receptor in innate immunity ofinvertebrates. In this study, a novel member of C1q-domain-containingprotein family was identified from Zhikong scallop Chlamys farreri(designated as CfC1qDC) by expressed sequence tag (EST) and rapidamplification of cDNA ends (RACE) approaches. The full-length cDNA ofCfC1qDC was of 777 bp, consisting of a 5'-terminal untranslated region(UTR) of 62 bp and a 3' UTR of 178 bp with a polyadenylation signalsequence AATAAA and a poly (A) tail. The CfC1qDC cDNA encoded apolypeptide of 178 amino acids, including a signal peptide and aC1q-domain of 158 amino acids with the theoretical isoelectric point of5.19 and the predicted molecular weight of 17.2 kDa. The C1q-domain inCfC1qDC exhibited homology with those in sialic acid binding lectin frommollusks and C1qDC proteins from higher vertebrates. The typical 10beta-strand jelly-roll folding topology structure of C1q-domain and theresidues essential for effective packing of the hydrophobic core were wellconserved in CfC1qDC. By fluorescent quantitative real-time PCR, mRNAtranscripts of CfC1qDC were mainly detected in kidney, mantle, adductormuscle and gill, and also marginally detectable in hemocytes. In thebacterial challenge experiment, after the scallops were challenged byListonella anguillarum, there was a significant up-regulation in therelative expression level of CfC1qDC and at 6h post-injection, the mRNAexpression reached the maximum level and was 4.55-fold higher than that ofcontrol scallops. Similarly, the expression of CfC1qDC mRNA in mixedprimary cultures of hemocytes stimulated by lipopolysaccharides (LPS) wasup-regulated and reached the maximum level at 6h post-stimulation, andthen dropped back to the original level gradually. In order to investigateits function, the cDNA fragment encoding the mature peptide of CfC1qDC wasrecombined and expressed in Escherichia coli BL21(DE3). The recombinantCfC1qDC protein displayed a significantly strong activity to bind LPS fromE. coli, although no obvious antibacterial or agglutinating activitytoward Gram-negative bacteria E. coli JM109, L. anguillarum andGram-positive bacteria Micrococcus luteus was observed. These resultssuggested that CfC1qDC was absolutely a novel member of the C1qDC proteinfamily and was involved in the recognition of invading microorganismsprobably as a pattern recognition molecule in mollusk.
- Baillat G et al.
- Molecular cloning and characterization of phocein, a protein found fromthe Golgi complex to dendritic spines.
- Mol Biol Cell. 2001; 12: 663-73
- Display abstract
Phocein is a widely expressed, highly conserved intracellular protein of225 amino acids, the sequence of which has limited homology to the sigmasubunits from clathrin adaptor complexes and contains an additionalstretch bearing a putative SH3-binding domain. This sequence isevolutionarily very conserved (80% identity between Drosophilamelanogaster and human). Phocein was discovered by a yeast two-hybridscreen using striatin as a bait. Striatin, SG2NA, and zinedin, the threemammalian members of the striatin family, are multimodular, WD-repeat, andcalmodulin-binding proteins. The interaction of phocein with striatin,SG2NA, and zinedin was validated in vitro by coimmunoprecipitation andpull-down experiments. Fractionation of brain and HeLa cells showed thatphocein is associated with membranes, as well as present in the cytosolwhere it behaves as a protein complex. The molecular interaction betweenSG2NA and phocein was confirmed by their in vivo colocalization, asobserved in HeLa cells where antibodies directed against either phocein orSG2NA immunostained the Golgi complex. A 2-min brefeldin A treatment ofHeLa cells induced the redistribution of both proteins. Immunocytochemicalstudies of adult rat brain sections showed that phocein reactivity,present in many types of neurons, is strictly somato-dendritic and extendsdown to spines, just as do striatin and SG2NA.
- Carty SM, Goldstrohm AC, Sune C, Garcia-Blanco MA, Greenleaf AL
- Protein-interaction modules that organize nuclear function: FF domains ofCA150 bind the phosphoCTD of RNA polymerase II.
- Proc Natl Acad Sci U S A. 2000; 97: 9015-20
- Display abstract
An approach for purifying nuclear proteins that bind directly to thehyperphosphorylated C-terminal repeat domain (CTD) of RNA polymerase IIwas developed and used to identify one human phosphoCTD-associatingprotein as CA150. CA150 is a nuclear factor implicated in transcriptionelongation. Because the hyperphosphorylated CTD is a feature of activelytranscribing RNA polymerase II (Pol II), phosphoCTD (PCTD) binding placesCA150 in a location appropriate for performing a role in transcriptionelongation-related events. Several recombinant segments of CA150 bound thePCTD. Predominant binding is mediated by the portion of CA150 containingsix FF domains, compact modules of previously unknown function. In fact,small recombinant proteins containing the fifth FF domain bound the PCTD.PCTD binding is the first specific function assigned to an FF domain. AsFF domains are found in a variety of nuclear proteins, it is likely thatsome of these proteins are also PCTD-associating proteins. Thus FF domainsappear to be compact protein-interaction modules that, like WW domains,can be evolutionarily shuffled to organize nuclear function.
- Misra S, Beach BM, Hurley JH
- Structure of the VHS domain of human Tom1 (target of myb 1): insights intointeractions with proteins and membranes.
- Biochemistry. 2000; 39: 11282-90
- Display abstract
VHS domains are found at the N-termini of select proteins involved inintracellular membrane trafficking. We have determined the crystalstructure of the VHS domain of the human Tom1 (target of myb 1) protein to1.5 A resolution. The domain consists of eight helices arranged in asuperhelix. The surface of the domain has two main features: (1) a basicpatch on one side due to several conserved positively charged residues onhelix 3 and (2) a negatively charged ridge on the opposite side, formed byresidues on helix 2. We compare our structure to the recently obtainedstructure of tandem VHS-FYVE domains from Hrs [Mao, Y., Nickitenko, A.,Duan, X., Lloyd, T. E., Wu, M. N., Bellen, H., and Quiocho, F. A. (2000)Cell 100, 447-456]. Key features of the interaction surface between theFYVE and VHS domains of Hrs, involving helices 2 and 4 of the VHS domain,are conserved in the VHS domain of Tom1, even though Tom1 does not have aFYVE domain. We also compare the structures of the VHS domains of Tom1 andHrs to the recently obtained structure of the ENTH domain of epsin-1[Hyman, J., Chen, H., Di Fiore, P. P., De Camilli, P., and Brunger, A. T.(2000) J. Cell Biol. 149, 537-546]. Comparison of the two VHS domains andthe ENTH domain reveals a conserved surface, composed of helices 2 and 4,that is utilized for protein-protein interactions. In addition, VHSdomain-containing proteins are often localized to membranes. We suggestthat the conserved positively charged surface of helix 3 in VHS and ENTHdomains plays a role in membrane binding.