The TRANSPARENT TESTA GLABRA1 ( TTG1 ) locus regulates several developmental and biochemical pathways in Arabidopsis, including the formation of hairs on leaves, stems, and roots, and the production of seed mucilage and anthocyanin pigments. The TTG1 locus has been isolated by positional cloning, and its identity was confirmed by complementation of a ttg1 mutant. The locus encodes a protein of 341 amino acid residues with four WD40 repeats. The protein is similar to AN11, a regulator of anthocyanin biosynthesis in petunia, and more distantly related to those of the ␤ subunits of heterotrimeric G proteins, which suggests a role for TTG1 in signal transduction to downstream transcription factors. The 1.5-kb TTG1 transcript is present in all major organs of Arabidopsis. Sequence analysis of six mutant alleles has identified base changes producing truncations or single amino acid changes in the TTG1 protein. INTRODUCTIONThe TRANSPARENT TESTA GLABRA1 ( TTG1 ) locus controls many apparently unrelated characters of Arabidopsis (catalogued by Koornneef, 1981), several of which appear to be confined to the epidermal cell layer of different tissues. ttg1 mutants have a glabrous phenotype, possessing none of the leaf or stem hairs (trichomes) that normally are derived from the meristematic L1 cell layer. Purple anthocyanin pigments are absent from the ttg1 seed coat, causing the transparent testa phenotype in which the yellow cotyledons are visible through the testa. In wild-type plants, anthocyanins are present in the hypocotyl of seedlings and in the stem and leaves of plants as they age, and they are inducible by many forms of stress, including high light, poor nutrients, or water stress. ttg1 mutants completely lack anthocyanins in the epidermis and in subepidermal layers of leaves and stems. Mucilage normally found in the cell wall of the seed coat is absent in ttg1 mutants. Seeds of ttg1 plants do not require drying and cold treatments to germinate and therefore exhibit an altered seed dormancy when compared with ecotypes, such as Landsberg erecta (L er ;Koornneef, 1981;Léon-Kloosterziel et al., 1994). This characteristic of ttg1 mutants may be linked to an altered seed coat structure. The TTG1 gene appears to have the opposite effect on root hair formation when compared with its effect on leaf hair initiation. In Arabidopsis, root hairs extend from root epidermal cells only in files of cells that contact two underlying cortical cells, whereas in ttg1 mutants, extra root hairs occur in the atrichoblast cell files (Galway et al., 1994). Under laboratory growth conditions, mutations at the ttg1 locus do not greatly affect the viability of the plants.In ttg1 mutants, the anthocyanin biosynthetic pathway is blocked at the dihydroflavonol-4-reductase (DFR) step, because DFR-encoding transcripts have not been detected in these mutants (Shirley et al., 1995). By contrast, transcripts of the chalcone synthase and chalcone isomerase genes are unaffected. The point of regulation of the pathway by TTG1 was confirmed by the clon...

The TCP transcription factors control multiple developmental traits in diverse plant species. Members of this family share an ;60-residue-long TCP domain that binds to DNA. The TCP domain is predicted to form a basic helix-loop-helix (bHLH) structure but shares little sequence similarity with canonical bHLH domain. This classifies the TCP domain as a novel class of DNA binding domain specific to the plant kingdom. Little is known about how the TCP domain interacts with its target DNA. We report biochemical characterization and DNA binding properties of a TCP member in Arabidopsis thaliana, TCP4. We have shown that the 58-residue domain of TCP4 is essential and sufficient for binding to DNA and possesses DNA binding parameters comparable to canonical bHLH proteins. Using a yeast-based random mutagenesis screen and sitedirected mutants, we identified the residues important for DNA binding and dimer formation. Mutants defective in binding and dimerization failed to rescue the phenotype of an Arabidopsis line lacking the endogenous TCP4 activity. By combining structure prediction, functional characterization of the mutants, and molecular modeling, we suggest a possible DNA binding mechanism for this class of transcription factors.

Protein kinases are central to regulation of cellular signaling in the eukaryotes. Wellconserved and lineage-specific protein kinases have previously been identified from various completely sequenced genomes of eukaryotes. The current work describes a genome-wide analysis for protein kinases encoded in the Plasmodium falciparum genome. Using a few different profile matching methods, we have identified 99 protein kinases or related proteins in the parasite genome. We have classified these kinases into subfamilies and analyzed them in the context of noncatalytic domains that occur in these catalytic kinase domain-containing proteins.

Pentraxins, which include C reactive protein (CRP) and serum amyloid P component (SAP), are prototypic acute phase reactants that serve as indicators of inflammatory reactions. Here we report genomic and cDNA cloning of mouse ptx3 (mptx3), a member of the pentraxin gene family and characterize its extrahepatic expression in vitro and in vivo. mptx3 is organized into three exons on chromosome 3: the first (43 aa) and second exon (175 aa) code for the signal peptide and for a protein portion with no high similarity to known sequences the third (203 aa) for a domain related to classical pentraxins, which contains the “pentraxin family signature.” Analysis of the N terminal portion predicts a predominantly alpha helical structure, while the pentraxin domain of ptx3 is accommodated comfortably in the tertiary structure fold of SAP. Normal and transformed fibroblasts, undifferentiated and differentiated myoblasts, normal endothelial cells, and mononuclear phagocytes express mptx3 mRNA and release the protein in vitro on exposure to interleukin-1beta (IL-1beta) and tumor necrosis factor (TNF)alpha. mptx3 was induced by bacterial lipopolysaccharide in vivo in a variety of organs and, most strongly, in the vascular endothelium of skeletal muscle and heart. Thus, mptx3 shows a distinct pattern of in vivo expression indicative of a significant role in cardiovascular and inflammatory pathology.

Symmetry is commonly observed in many biological systems. Here we discuss representative examples of the role of symmetry in structural molecular biology. Point group symmetries are observed in many protein oligomers whose three-dimensional atomic structures have been elucidated by x-ray crystallography. Approximate symmetry also occurs in multidomain proteins. Symmetry often confers stability on the molecular system and results in economical usage of basic components to build the macromolecular structure. Symmetry is also associated with cooperativity.