B. Rajendra Krishnan

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The initial steps in assimilation of sulfate during cysteine biosynthesis entail sulfate uptake and sulfate activation by formation of adenosine 5'-phosphosulfate, conversion to 3'-phosphoadenosine 5'-phosphosulfate, and reduction to sulfite. Mutations in a previously uncharacterized Escherichia coli gene, cysQ, which resulted in a requirement for sulfite(More)
The class I region of the human leukocyte antigen (HLA) complex located on chromosome 6p21.3 is gene dense. To define the gene content of the class I region, we are constructing genomic DNA feature maps. Here we report mapping of the POU5F1 and TCF19 genes to an approximately 0.2-Mb region between the HLA-C and the S genes. Localization of these genes was(More)
Animal globin genes have two introns at strictly conserved positions, while plant globin genes have both of these as well as an additional, central intron. It has been proposed that a common ancestor gene had three introns, one of which was subsequently lost from animal but not plant globin genes. We have elucidated the cDNA sequence and gene structure of a(More)
We have designed "split tetra-Cys motifs" that bind the biarsenical fluorescein dye 4',5'-bis(1,3,2-dithioarsolan-2-yl)fluorescein (FlAsH) across strands of a model beta-rich protein. Our strategy was to divide the linear FlAsH binding tetra-Cys sequence such that dye could be fully liganded only when the strands were arranged in space correctly by native(More)
A crucial challenge in present biomedical research is the elucidation of how fundamental processes like protein folding and aggregation occur in the complex environment of the cell. Many new physico-chemical factors like crowding and confinement must be considered, and immense technical hurdles must be overcome in order to explore these processes in vivo.(More)
The conformational plasticity of serine protease inhibitors (serpins) underlies both their activities as protease inhibitors and their susceptibility to pathogenic misfolding and aggregation. Here, we structurally characterize a sheet-opened state of the serpin α-1 antitrypsin (α₁AT) and show how local unfolding allows functionally essential strand(More)
In Escherichia coli, the cytosolic chaperone SecB is responsible for the selective entry of a subset of precursor proteins into the Sec pathway. In vitro, SecB binds to a variety of unfolded substrates without apparent sequence specificity, but not native proteins. Selectivity has therefore been suggested to occur by kinetic partitioning of substrates(More)
The SecA molecular nanomachine in bacteria uses energy from ATP hydrolysis to drive post-translational secretion of preproteins through the SecYEG translocon. Cytosolic SecA exists in a dimeric, "closed" state with relatively low ATPase activity. After binding to the translocon, SecA undergoes major conformational rearrangement, leading to a state that is(More)
Coupling genetically encoded target sequences with specific and selective labeling strategies has made it possible to utilize fluorescence spectroscopy in complex mixtures to investigate the structure, function, and dynamics of proteins. Thus, there is a growing need for a repertoire of such labeling approaches to deploy based on a given application and to(More)