Isolation and characterization of the Neurospora crassa endoplasmic reticulum.

Abstract:

:The endoplasmic reticulum from Neurospora crassa was identified by monitoring the activity of the putative enzyme marker phosphatidylcholine glyceride transferase. After differential centrifugation of a cell homogenate, phosphatidylcholine glyceride transferase activity initially copurified with plasma membrane H+-ATPase. However, isopycnic centrifugation of the whole-cell homogenate on a linear sucrose gradient separated the two enzyme activities into different fractions. The lighter membrane fraction exhibited characteristics that have been associated with the endoplasmic reticulum in other organisms: (i) the inclusion of magnesium caused this light membrane fraction to shift to a higher density on the gradient; (ii) it was highly enriched in cytochrome c reductase, an endoplasmic reticulum marker in other systems; and (iii) the morphology of the light fraction with and without added magnesium was clearly distinguishable from that of the plasma membrane fraction by electron microscopy. A reinvestigation of the location of chitin synthetase confirmed its association with the plasma membrane fraction even after separation of the lighter fractions.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Borgeson CE,Bowman BJ

doi

10.1128/JB.156.1.362-368.1983

subject

Has Abstract

pub_date

1983-10-01 00:00:00

pages

362-8

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

156

pub_type

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