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PASS Scripta Varia 21 - Pontifical Academy of Sciences

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INTRACELLULAR PROTEIN DEGRADATION<br />

Figure 3: APF-1/Ubiquitin is shifted to high molecular mass compound(s) following incubation<br />

in ATP-containing crude cell extract. 125 I-labelled APF-1/ ubiquitin was incubated with reticulocyte<br />

crude Fraction II in the absence (open circles) or presence (closed circles) <strong>of</strong> ATP, and the reaction<br />

mixtures were resolved via gel filtration chromatography. Shown is the radioactivity measured in<br />

each fraction. As can be seen, following addition <strong>of</strong> ATP, APF-1/ubiquitin becomes covalently attached<br />

to some component(s) in fraction II, which could be another enzyme <strong>of</strong> the system or its<br />

substrate(s) (with permission from Proceedings <strong>of</strong> the National <strong>Academy</strong> <strong>of</strong> the USA; published<br />

originally in Ref. 39).<br />

these organisms (unpublished) showed that ubiquitin is restricted only to eukaryotes.<br />

The finding <strong>of</strong> ubiquitin in bacteria (44) was probably due to contamination<br />

<strong>of</strong> the bacterial extract with yeast ubiquitin derived from the yeast<br />

extract in which the bacteria were grown. While in retrospect the name ubiquitin<br />

is a misnomer, as it is restricted to eukaryotes and is not ubiquitous as<br />

was previously thought, for historical reasons it has still remained the name <strong>of</strong><br />

the protein. Accordingly, and in order to avoid confusion, I suggest that the<br />

names <strong>of</strong> other novel enzymes and components <strong>of</strong> the ubiquitin system, but<br />

<strong>of</strong> other systems as well, should remain as were first coined by their discoverers.<br />

The Scientific Legacy <strong>of</strong> the 20 th Century<br />

299

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