Mechanism of Excretion of a Bacterial Proteinase: Demonstration of Two Proteolytic Enzymes Produced by a Sarcina Strain (Coccus P)

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A Sarcina strain (Coccus P) produces two proteolytic enzymes. One is found only extracellularly, is far more prevalent, and is actively excreted during exponential growth. It is the enzyme responsible for the known strong proteolytic activity of the cultures of this strain. A second protease is, however, produced which remains associated with the intact cells but is released by the protoplasts. The two enzymes appear unrelated in their derivation. Calcium ions play an essential role in preventing autodigestion of the excreted enzyme. Bacterial proteins are found outside the cell boundary as a consequence either of passive processes such as leakage ... continued below

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SARNER, NITZA Z; BISSELL, MINA J; GIROLAMO, MARIO Di & GORINI, LUIGI June 29, 1970.

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A Sarcina strain (Coccus P) produces two proteolytic enzymes. One is found only extracellularly, is far more prevalent, and is actively excreted during exponential growth. It is the enzyme responsible for the known strong proteolytic activity of the cultures of this strain. A second protease is, however, produced which remains associated with the intact cells but is released by the protoplasts. The two enzymes appear unrelated in their derivation. Calcium ions play an essential role in preventing autodigestion of the excreted enzyme. Bacterial proteins are found outside the cell boundary as a consequence either of passive processes such as leakage or lysis or of active excretion. Under conditions in which leakage and lysis do not occur, as during exponential growth, the cell boundary is a barrier causing a complete separation of the bulk of the intracellular proteins from the one or very few extracellular proteins, with no trace of either type being detectable on the wrong side of the boundary. Since in bacteria there is no evidence of protein being produced other than internally, the separation into intraand extracellular proteins should occur after peptide chain formation. The question arises as to whether the structure of the cell boundary or that of the excreted proteins themselves determines this separation. Coccus P, a Sarcina closely related to Micrococcus lysodeikticus (3), produces an extracellular proteinase during the exponential phase of growth so that the process appears to be active excretion. The organism grows exponentially in a defined synthetic medium (12) to relatively high cell density (10{sup 9} cells/ml); therefore the mechanism of excretion can be studied over an extended period of time without the difficulties of changing growth rates. Coagulation of reconstituted skim milk provides a simple and sensitive assay for enzyme activity (I 1). The extracellular proteinase has also been purified and partially characterized (6-8). It has been shown that extracellular proteolytic activity can be found only when Ca{sup 2+} is present in the medium (4). However, there is always a low level of proteolytic activity associated with the cells irrespective of the presence of Ca{sup 2+}. This paper is concerned with the relation between these two extra- and intracellular proteolytic activities. It is found that they are due to two different proteins, only one of which is actively excreted.

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  • Journal Name: Journal of Bacteriology; Journal Volume: 105; Journal Issue: 3; Related Information: Journal Publication Date: 3/1/1971

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  • Report No.: LBNL-4375E
  • Grant Number: DE-AC02-05CH11231
  • Grant Number: 5 ROI Al 02011-12
  • Office of Scientific & Technical Information Report Number: 1009843
  • Archival Resource Key: ark:/67531/metadc829361

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  • June 29, 1970

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  • May 19, 2016, 3:16 p.m.

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  • June 16, 2016, 12:46 p.m.

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SARNER, NITZA Z; BISSELL, MINA J; GIROLAMO, MARIO Di & GORINI, LUIGI. Mechanism of Excretion of a Bacterial Proteinase: Demonstration of Two Proteolytic Enzymes Produced by a Sarcina Strain (Coccus P), article, June 29, 1970; Berkeley, California. (digital.library.unt.edu/ark:/67531/metadc829361/: accessed April 21, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.