Secondary literature sources for LCCL
The following references were automatically generated.
- Malgieri G et al.
- The prokaryotic Cys2His2 zinc-finger adopts a novel fold as revealed bythe NMR structure of Agrobacterium tumefaciens Ros DNA-binding domain.
- Proc Natl Acad Sci U S A. 2007; 104: 17341-6
- Display abstract
The first putative prokaryotic Cys(2)His(2) zinc-finger domain has beenidentified in the transcriptional regulator Ros from Agrobacteriumtumefaciens, indicating that the Cys(2)His(2) zinc-finger domain,originally thought to be confined to the eukaryotic kingdom, could bewidespread throughout the living kingdom from eukaryotic, both animal andplant, to prokaryotic. In this article we report the NMR solutionstructure of Ros DNA-binding domain (Ros87), providing 79 structuralcharacterization of a prokaryotic Cys(2)His(2) zinc-finger domain. The NMRstructure of Ros87 shows that the putative prokaryotic Cys(2)His(2)zinc-finger sequence is indeed part of a significantly larger zinc-bindingglobular domain that possesses a novel protein fold very different fromthe classical fold reported for the eukaryotic classical zinc-finger. TheRos87 globular domain consists of 58 aa (residues 9-66), is arranged in abetabetabetaalphaalpha topology, and is stabilized by an extensive15-residue hydrophobic core. A backbone dynamics study of Ros87, based on(15)N R(1), (15)N R(2), and heteronuclear (15)N-{(1)H}-NOE measurements,has further confirmed that the globular domain is uniformly rigid andflanked by two flexible tails. Mapping of the amino acids necessary forthe DNA binding onto Ros87 structure reveals the protein surface involvedin the DNA recognition mechanism of this new zinc-binding protein domain.
- Bhattacharya SK, Peachey NS, Crabb JW
- Cochlin and glaucoma: a mini-review.
- Vis Neurosci. 2005; 22: 605-13
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Primary open angle glaucoma (POAG) is a leading cause of late onset,progressive, irreversible blindness and, although its etiology is poorlyunderstood, elevated intraocular pressure (IOP) often appears to be acontributory factor. Proteomic and Western analyses of trabecular meshwork(TM) from patients with POAG and age-matched controls originallyimplicated cochlin as possibly contributing to glaucoma pathogenesis.Cochlin deposits were subsequently detected in glaucomatous but not incontrol TM and older glaucomatous TM was found to contain higher levels ofcochlin and significantly lower amounts of collagen type II. Morerecently, similar results were reported in DBA/2J mice, which at olderages develop elevated IOP, retinal ganglion cell degeneration, and opticnerve damage. Notably, cochlin was absent in TM from C57BL/6J, CD1, andBALBc/ByJ mice, which do not exhibit elevated IOP or glaucoma. Cochlin wasfound in the TM of very young DBA/2J mice, prior to elevated IOP,suggesting that over time the protein may contribute to the events leadingto increased IOP and optic nerve damage. Here we review these findings anddescribe how future studies in DBA/2J mice can help resolve whethercochlin plays a causal role in mechanisms of POAG and elevated IOP.
- Yin L et al.
- Crystal structure of human SH3BGRL protein: the first structure of thehuman SH3BGR family representing a novel class of thioredoxin foldproteins.
- Proteins. 2005; 61: 213-6
- Jawhari A et al.
- Domain architecture of the p62 subunit from the human transcription/repairfactor TFIIH deduced by limited proteolysis and mass spectrometryanalysis.
- Biochemistry. 2004; 43: 14420-30
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TFIIH is a multiprotein complex that plays a central role in bothtranscription and DNA repair. The subunit p62 is a structural component ofthe TFIIH core that is known to interact with VP16, p53, Eralpha, and E2F1in the context of activated transcription, as well as with theendonuclease XPG in DNA repair. We used limited proteolysis experimentscoupled to mass spectrometry to define structural domains within theconserved N-terminal part of the molecule. The first domain identifiedresulted from spontaneous proteolysis and corresponds to residues 1-108.The second domain encompasses residues 186-240, and biophysicalcharacterization by fluorescence studies and NMR analysis indicated thatit is at least partially folded and thus may correspond to a structuralentity. This module contains a region of high sequence conservation withan invariant FWxxPhiPhi motif (Phi representing either tyrosine orphenylalanine), which was also found in other protein families and couldplay a key role as a protein-protein recognition module within TFIIH. Theapproach used in this study is general and can be straightforwardlyapplied to other multidomain proteins and/or multiprotein assemblies.
- Niderman T et al.
- Pathogenesis-related PR-1 proteins are antifungal. Isolation andcharacterization of three 14-kilodalton proteins of tomato and of a basicPR-1 of tobacco with inhibitory activity against Phytophthora infestans.
- Plant Physiol. 1995; 108: 17-27
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Three distinct basic 14-kD proteins, P14a, P14b, and P14c, were isolatedfrom tomato (Lycopersicon esculentum Mill. cv Baby) leaves infected withPhytophthora infestans. They exhibited antifungal activity against P.infestans both in vitro (inhibition of zoospore germination) and in vivowith a tomato leaf disc assay (decrease in infected leaf surface).Serological cross-reactions and amino acid sequence comparisons showedthat the three proteins are members of the PR-1 group ofpathogenesis-related (PR) proteins. P14a and P14b showed high similarityto a previously characterized P14, whereas P14c was found to be verysimilar to a putative basic-type PR-1 from tobacco predicted from isolatedDNA clones. This protein, named PR-1 g, was purified from virus-infectedtobacco (Nicotiana tabacum Samsun NN) leaves and characterized by aminoacid microsequencing, along with the well-known acidic tobacco PR-1a,PR-1b, and PR-1c. The various tomato and tobacco PR-1 proteins werecompared for their biological activity and found to display differentialfungicidal activity against P. infestans in both the in vitro and in vivoassays, the most efficient being the newly characterized tomato P14c andtobacco PR-1g.