Spatial Pattern Templates for Recognition of Objects with Regular Structure

1999 ◽

Vol 29 (2) ◽

pp. 202-212 ◽

Cited By ~ 30

Author(s):

Carol Miller ◽

Dean L Urban

Keyword(s):

Spatial Heterogeneity ◽

Spatial Pattern ◽

Sierra Nevada ◽

Fire Regime ◽

Regular Structure ◽

Fire Regimes ◽

Surface Fire ◽

Surface Fires ◽

Crown Fires ◽

Wide Range

Fire is a major agent of spatial pattern formation in forests, as it creates a mosaic of burned and unburned patches. While most research has focused on landscape-level patterns created by crown fires, millions of hectares of forests in North America are subject to surface fire regimes. A spatially explicit forest gap model developed for the Sierra Nevada was used to evaluate the influence of surface fire regimes on the heterogeneity of forest structure and composition within forest stands. Forest pattern was evaluated for a wide range of topographic positions in Sequoia National Park, California, to determine if repeated surface fires amplify existing spatial patterns. The spatial heterogeneity of some forest characteristics increased under a simulated fire regime relative to scenarios without fire. Although a distinct and regular fire-generated spatial pattern was not detected with an analysis of spatial autocorrelation, simulated surface fires did alter the spatial heterogeneity within a forest stand, primarily by degrading a regular structure that is imposed by competition for light in the absence of fire. The interaction between surface fires and forest pattern may be qualitatively different from that which occurs in forests subject to crown fires. As such, what has been learned about forests dominated by crown fires may not apply to forests subject to surface fire regimes.

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Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100123969 ◽

1992 ◽

Vol 50 (1) ◽

pp. 712-713

Author(s):

Xiaorong Zhu ◽

Richard McVeigh ◽

Bijan K. Ghosh

Keyword(s):

Alkaline Phosphatase ◽

Bacillus Licheniformis ◽

Self Assembly ◽

Gel Electrophoresis ◽

Culture Supernatant ◽

Regular Structure ◽

The Self ◽

Cellular Distribution ◽

Structural Protein ◽

Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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