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The characteristics of 2',4',5',7'-tetrabromoflourescein is discussed in terms of its usefulness as anefficient photosensitizer in the selection of new mutants of endocytosis. I2FD and Br4FD could both produce singlet oxygen as shown by their abilities to mediate bleaching of p-nitrosoaniline in the presence of histidine. Intracellular uptake of Br4FD showed that it could be used as a fluid phase marker in D. amoebae. Br4FD was three times more efficient than I2FD in terms of photosensitizer effectivity.

Presents a study which cloned and sequenced the gene encoding the Dictyostelium discoideum (D. discoideum) mitochondrial adenine nucleotide translocator (ANT) and analyzed its transcriptional regulation. Information on ANT; Cell cultures and isolation of D. discoideum mitochondria; Immunological detection of D. discoideum ANT.

A product of mitochondrial protein synthesis in rat liver mitochondria, characterized by a low molecular weight (Mr < 10000) and an unusually high hydrophobicity, has been identified as the dicyclohexylcarbodiimide-binding protein and as a peptide of the hydrophobic sector of the mitochondrial ATPase complex. The purified protein still possesses the ability to bind dicyclohexylcarbodiimide. [ABSTRACT FROM AUTHOR]

A low molecular weight product (Mr 7000) synthetized on rat liver mitoribosomes is selectively extracted by chloroform/methanol (&frac21;). This products characterized by an unusual hydrophobicity, as reflected by its chromatographic behaviour, its high content in hydrophobic amino acids and its strong capacity to bind lipids. Bound lipids contain a high percentage of linoleic acid. [ABSTRACT FROM AUTHOR]

I. This paper describes some features of the protein synthesis in isolated rat liver mitochondria and reports on the stability of the product of mitochondrial protein synthesis in vitro. 2. Chase experiments performed after a 30-min pulse of [14C]leucine indicated that a large part of the product is degraded to an acid-soluble form (labile product) almost as rapidly as it is terminated and released from the mitoribosome. Only a small proportion of the completed product (between 20 and 40 %)is conversed in acid-insoluble form (stable product). 2. Both labile and stable products have an exceptional degree of hydrophobicity, shown by their marked resistance to acid and alkaline hydrolysis and by their solubility in organic solvents. 4. A 14C-labelled peptide with an apparent molecular weight of 12000-13000, as assessed by gel electrophoresis in the presence of dodecylsulfate, is released after heat treatment of mitoribosomes isolated from mitochondria pulsed with [14C]leucine. [ABSTRACT FROM AUTHOR]