ERTS-1 applications to Minnesota land use mapping

Land use class definitions that can be operationally employed with ERTS-1 imagery are being developed with the cooperation of personnel from several state, regional, and federal agencies with land management responsibilities within the state and the University of Minnesota. Investigations of urban, extractive, forest, and wetlands areas indicate that it is feasible to subdivide each of these classes into several sub-classes with the use of ERTS-1 images from one or more time periods

Application of ERTS-1 imagery to state wide land information system in Minnesota

There are no author-identified significant results in this report

Aerial Photo Detection of Highway-Associated Damage to Red Pine

Published as Scientific Journal Paper Series No. 8113 of the Minnesota Agricultural Experiment Station

Defining a Key Receptor–CheA Kinase Contact and Elucidating Its Function in the Membrane-Bound Bacterial Chemosensory Array: A Disulfide Mapping and TAM-IDS Study

The three core components of the ubiquitous bacterial chemosensory array  the transmembrane chemoreceptor, the histidine kinase CheA, and the adaptor protein CheW  assemble to form a membrane-bound, hexagonal lattice in which receptor transmembrane signals regulate kinase activity. Both the regulatory domain of the kinase and the adaptor protein bind to overlapping sites on the cytoplasmic tip of the receptor (termed the protein interaction region). Notably, the kinase regulatory domain and the adaptor protein share the same fold constructed of two SH3-like domains. The present study focuses on the structural interface between the receptor and the kinase regulatory domain. Two models have been proposed for this interface: Model 1 is based on the crystal structure of a homologous Thermotoga complex between a receptor fragment and the CheW adaptor protein. This model has been used in current models of chemosensory array architecture to build the receptor–CheA kinase interface. Model 2 is based on a newly determined crystal structure of a homologous Thermotoga complex between a receptor fragment and the CheA kinase regulatory domain. Both models present unique strengths and weaknesses, and current evidence is unable to resolve which model best describes contacts in the native chemosensory arrays of <i>Escherichia coli</i>, <i>Salmonella typhimurium</i>, and other bacteria. Here we employ disulfide mapping and tryptophan and alanine mutation to identify docking sites (TAM-IDS) to test Models 1 and 2 in well-characterized membrane-bound arrays formed from <i>E. coli</i> and <i>S. typhimurium</i> components. The results reveal that the native array interface between the receptor protein interaction region and the kinase regulatory domain is accurately described by Model 2, but not by Model 1. In addition, the results show that the interface possesses both a structural function that contributes to stable CheA kinase binding in the array and a regulatory function central to transmission of the activation signal from receptor to CheA kinase. On–off switching alters the disulfide formation rates of specific Cys pairs at the interface, but not most Cys pairs, indicating that signaling perturbs localized regions of the interface. The findings suggest a simple model for the rearrangement of the interface triggered by the attractant signal and for longer range transmission of the signal in the chemosensory array