Disease relevance of rpi

• Rhizobium meliloti C4-dicarboxylic acid transport protein D (DCTD) activates transcription by a form of RNA polymerase holoenzyme that has sigma 54 as its sigma factor (referred to as E sigma 54) [1].
• Protein D of molecular weight 80,000 is incorporated into the membrane of Escherichia coli B/r for a brief fraction of the cell cycle [2].
• The gene encoding protein D (hpd) is highly conserved among Haemophilus influenzae type b and nontypeable strains [3].
• Protein D is 64 and 36% identical and 77 and 56% similar to the glycerophosphodiester phosphodiesterases (GlpQ) of Escherichia coli and Bacillus subtilis [3].
• Protein D is also an established fusion partner for phage display [4].

High impact information on rpi

• In synchronous acetate-grown cultures a 10-fold increase in the rate of protein D synthesis occurs toward the end of the cell cycle, near the end of one round of DNA synthesis and the start of the next [2].
• The addition of beta-lactam antibiotics which affect murein metabolism dramatically increases the amount of protein D. The cells are prevented from terminating protein D synthesis; different antibiotics have different kinetics of action [2].
• The synthesis of both protein D and DNA is prevented by nalidixic acid; after its removal a sharp spike of protein D synthesis is followed by a wave of DNA synthesis [2].
• Surfactant Protein D Augments Bacterial Association but Attenuates Major Histocompatibility Complex Class II Presentation of Bacterial Antigens [5].
• The nucleotide sequences and the deduced amino acid sequences for protein D were highly conserved [3].

Chemical compound and disease context of rpi

• Protein D has previously been demonstrated to be associated with Escherichia coli ribosomes by the radical-free and highly reducing method of two-dimensional polyacrylamide gel electrophoresis [6].

Biological context of rpi

• In the deduced amino acid sequences for protein D, only 2 of 364 amino acid residues differed [7].
• Surfactant protein D enhances bacterial antigen presentation by bone marrow-derived dendritic cells [8].
• Instead, the region upstream of cmi contained sequences that showed 91% homology to the structural gene of protein D (resolvase) and 75.5% homology to the rfsF sequence of the Escherichia coli miniF plasmid [9].
• Preliminary observations on one of the proteins of the heat shock response, protein D 48.5, suggested that its induction by sigma-32 during heat shock may be modulated by catabolite repression [10].

Associations of rpi with chemical compounds

• A mutant expressing a protein D lacking the cysteine residue was constructed by oligonucleotide site-directed mutagenesis [11].
• The mutated protein D molecule was not acylated and partitioned in the aqueous phase after Triton X-114 extraction of intact bacteria, unlike native and recombinant protein D, which partitioned in the detergent phase [11].
• Globomycin inhibited maturation of protein D in H. influenzae, implying that protein D is exported through the lipoprotein export pathway [11].

Analytical, diagnostic and therapeutic context of rpi

• The CsCl density gradient centrifugation of high salt washed 70S ribosomes showed that protein A belonged to the insoluble split proteins, proteins B and C to the core particles, and protein D and a small population of B to the soluble split proteins [12].

References