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Eukaryotic cells typically contain 0.2-1.0% of their total protein as the highly conserved protein ubiquitin, which exists both free and covalently attached to cellular proteins. The attachment of ubiquitin to cellular proteins occurs posttranslationally by a three-enzyme pathway and results in a peptide linkage of the C terminus of ubiquitin either to a lysyl epsilon-amino group of a substrate protein or to a lysyl epsilon-amino group of a previously linked ubiquitin molecule. The multiple conjugation of ubiquitin to substrate proteins via ubiquitin-ubiquitin linkages is thought to be necessary, but not sufficient, for recognition and degradation by a ubiquitin-dependent protease. In higher plant cells the steady-state level of ubiquitinated proteins is generally constant and can be readily detected in all somatic tissues. In contrast, we have found that a developmentally regulated loss of free ubiquitin and ubiquitinated proteins occurs during maize (Zea mays L.) pollen maturation. This dramatic loss of ubiquitin correlates temporally with commitment to the gametophytic developmental program. Northern blot analysis indicates that the loss of ubiquitin is not due to low levels of ubiquitin mRNA, suggesting that a posttranscriptional regulatory mechanism is responsible.

Developmentally regulated loss of ubiquitin and ubiquitinated proteins during pollen maturation in maize.