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Articles by Surobhi Lahiri
Total Records ( 3 ) for Surobhi Lahiri
  Surobhi Lahiri , Byron Cole , Lakshmi Pulakat and Nara Gavini
  The nitrogenase enzyme catalyzes the reduction of dinitrogen to ammonia and is composed of the Fe and MoFe proteins. The iron molybdenum cofactor (FeMo-co) of the MoFe protein is the site of active substrate reduction. The NifX protein has also been suggested to have a role in the FeMo-co synthesis, although its exact role is still open to investigation. We attempted to understand the role of NifX by determining the specific interactions it may have with other Nif proteins involved in FeMo-co synthesis, such as NifD, NifK, NifN, NifDK and NifH. Using the BacterioMatch Two-Hybrid System, a translationally fused construct of NifX with the N-terminal α-RNAP of the pTRG target vector was made and its interaction was tested with the NifDK fusion protein, translationally fused to the λCI of the pBT vector. The strength of the interaction, as determined by measuring the β-galactosidase activity, demonstrated that direct protein-protein interaction exists between NifDK and NifX proteins; the extent of interaction between NifK and NifX proteins was much higher than between NifD and NifX, when individually tested; also, reduced interaction was found between NifH and NifX.
  Surobhi Lahiri , Lakshmi Pulakat and Nara Gavini
  The NifH protein is a subunit of the nitrogenase enzyme that catalyzes the reduction of atmospheric nitrogen to ammonia. This protein contains highly conserved regions including the nucleotide binding sites, metal center ligands and the Switch I and Switch II domains. A number of proteins have structural and mechanistic similarities as well as evolutionary relationships with the NifH protein, notable among them being: light independent protochlorophyllide (Pchlide) reductase (ChlL/FrxC or bChL), arsenite pump ATPase (ArsA), 2-hydroxyglutaryl dehydratase Component A (CompA) involved in glutamate degradation and MinD that functions in spatial regulation of cell division. Although involved in very diverse biological processes, these proteins share an underlying common structural framework. This review mainly focuses on the structural similarities of these proteins with the NifH protein and discusses recent reports of complementation studies involving NifH and few of the proteins mentioned.
  W. Matthew Sattley , Michael T. Madigan , Wesley D. Swingley , Patricia C. Cheung , Kate M. Clocksin , Amber L. Conrad , Liza C. Dejesa , Barbara M. Honchak , Deborah O. Jung , Lauren E. Karbach , Ahmet Kurdoglu , Surobhi Lahiri , Stephen D. Mastrian , Lawrence E. Page , Heather L. Taylor , Zi T. Wang , Jason Raymond , Min Chen , Robert E. Blankenship and Jeffrey W. Touchman
  Despite the fact that heliobacteria are the only phototrophic representatives of the bacterial phylum Firmicutes, genomic analyses of these organisms have yet to be reported. Here we describe the complete sequence and analysis of the genome of Heliobacterium modesticaldum, a thermophilic species belonging to this unique group of phototrophs. The genome is a single 3.1-Mb circular chromosome containing 3,138 open reading frames. As suspected from physiological studies of heliobacteria that have failed to show photoautotrophic growth, genes encoding enzymes for known autotrophic pathways in other phototrophic organisms, including ribulose bisphosphate carboxylase (Calvin cycle), citrate lyase (reverse citric acid cycle), and malyl coenzyme A lyase (3-hydroxypropionate pathway), are not present in the H. modesticaldum genome. Thus, heliobacteria appear to be the only known anaerobic anoxygenic phototrophs that are not capable of autotrophy. Although for some cellular activities, such as nitrogen fixation, there is a full complement of genes in H. modesticaldum, other processes, including carbon metabolism and endosporulation, are more genetically streamlined than they are in most other low-G+C gram-positive bacteria. Moreover, several genes encoding photosynthetic functions in phototrophic purple bacteria are not present in the heliobacteria. In contrast to the nutritional flexibility of many anoxygenic phototrophs, the complete genome sequence of H. modesticaldum reveals an organism with a notable degree of metabolic specialization and genomic reduction.
 
 
 
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