The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP release. 2012

Sanchaita Das, and Lorry M Grady, and Jennifer Michtavy, and Yayan Zhou, and Frederick M Cohan, and Manju M Hingorani, and Donald B Oliver
Department of Molecular Biology and Biochemistry, Wesleyan University, Middletown, Connecticut, USA.

Bacterial SecA proteins can be categorized by the presence or absence of a variable subdomain (VAR) located within nucleotide-binding domain II of the SecA DEAD motor. Here we show that VAR is dispensable for SecA function, since the VAR deletion mutant secAΔ519-547 displayed a wild-type rate of cellular growth and protein export. Loss or gain of VAR is extremely rare in the history of bacterial evolution, indicating that it appears to contribute to secA function within the relevant species in their natural environments. VAR removal also results in additional secA phenotypes: azide resistance (Azi(r)) and suppression of signal sequence defects (PrlD). The SecAΔ(519-547) protein was found to be modestly hyperactive for SecA ATPase activities and displayed an accelerated rate of ADP release, consistent with the biochemical basis of azide resistance. Based on our findings, we discuss models whereby VAR allosterically regulates SecA DEAD motor function at SecYEG.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D010802 Phylogeny The relationships of groups of organisms as reflected by their genetic makeup. Community Phylogenetics,Molecular Phylogenetics,Phylogenetic Analyses,Phylogenetic Analysis,Phylogenetic Clustering,Phylogenetic Comparative Analysis,Phylogenetic Comparative Methods,Phylogenetic Distance,Phylogenetic Generalized Least Squares,Phylogenetic Groups,Phylogenetic Incongruence,Phylogenetic Inference,Phylogenetic Networks,Phylogenetic Reconstruction,Phylogenetic Relatedness,Phylogenetic Relationships,Phylogenetic Signal,Phylogenetic Structure,Phylogenetic Tree,Phylogenetic Trees,Phylogenomics,Analyse, Phylogenetic,Analysis, Phylogenetic,Analysis, Phylogenetic Comparative,Clustering, Phylogenetic,Community Phylogenetic,Comparative Analysis, Phylogenetic,Comparative Method, Phylogenetic,Distance, Phylogenetic,Group, Phylogenetic,Incongruence, Phylogenetic,Inference, Phylogenetic,Method, Phylogenetic Comparative,Molecular Phylogenetic,Network, Phylogenetic,Phylogenetic Analyse,Phylogenetic Clusterings,Phylogenetic Comparative Analyses,Phylogenetic Comparative Method,Phylogenetic Distances,Phylogenetic Group,Phylogenetic Incongruences,Phylogenetic Inferences,Phylogenetic Network,Phylogenetic Reconstructions,Phylogenetic Relatednesses,Phylogenetic Relationship,Phylogenetic Signals,Phylogenetic Structures,Phylogenetic, Community,Phylogenetic, Molecular,Phylogenies,Phylogenomic,Reconstruction, Phylogenetic,Relatedness, Phylogenetic,Relationship, Phylogenetic,Signal, Phylogenetic,Structure, Phylogenetic,Tree, Phylogenetic
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000069816 SEC Translocation Channels Universally conserved multiprotein complexes that form the protein transport channel of the general secretory (SEC) pathway. The SEC translocase is present in all bacteria, archaea, and eukaryotes. It is in the ENDOPLASMIC RETICULUM membrane of eukaryotic cells, in the THYLAKOID MEMBRANE in CHLOROPLASTS and in some protozoa in the INNER MITOCHONDRIAL MEMBRANE. SEC Translocation Channel,SEC Translocon,SEC61 Translocation Channel,Sec Protein Translocation System,SecYEG Protein,SecYEG Translocation Channel,SEC Complexes,SEC Translocase,SEC Translocons,SEC61 Protein,SEC61 Proteins,SEC61 Translocase,SEC61 Translocation Channels,SEC61 Translocon,Sec Protein Translocation Systems,Sec61 Complex,Sec61 Protein Translocation System,SecY Translocase,SecYEG Complex,SecYEG Complexes,SecYEG Protein Translocation System,SecYEG Proteins,SecYEG Translocation Channels,SecYEG Translocon,Channel, SEC Translocation,Channel, SEC61 Translocation,Channel, SecYEG Translocation,Channels, SEC Translocation,Channels, SEC61 Translocation,Channels, SecYEG Translocation,Complex, Sec61,Complex, SecYEG,Complexes, SEC,Complexes, SecYEG,Protein, SEC61,Protein, SecYEG,Proteins, SEC61,Proteins, SecYEG,Translocase, SEC,Translocase, SEC61,Translocase, SecY,Translocation Channel, SEC,Translocation Channel, SEC61,Translocation Channel, SecYEG,Translocation Channels, SEC,Translocation Channels, SEC61,Translocation Channels, SecYEG,Translocon, SEC,Translocon, SEC61,Translocon, SecYEG,Translocons, SEC
D000081416 SecA Proteins ATPases that provide energy for the translocation of proteins across bacterial PLASMA MEMBRANES and THYLAKOID membranes, by the SEC TRANSLOCATION CHANNELS. SecA is a component of the bacterial preprotein translocase which is comprised of SecA, the SECYEG TRANSLOCON, and the accessory domain proteins SecD, SecF, YajC, and YidC. SecA Protein,Protein, SecA,Proteins, SecA
D000244 Adenosine Diphosphate Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position. ADP,Adenosine Pyrophosphate,Magnesium ADP,MgADP,Adenosine 5'-Pyrophosphate,5'-Pyrophosphate, Adenosine,ADP, Magnesium,Adenosine 5' Pyrophosphate,Diphosphate, Adenosine,Pyrophosphate, Adenosine

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