The mitochondrial ribosomal protein MrpS28 of Saccharomyces cerevisiae is one of several mitochondrial ribosomal proteins homologous to Escherichia coli ribosomal proteins within the context of a larger protein. Relative to a region of homology with E. coli ribosomal protein S15, the mature MrpS28 protein has unique sequence domains of 117 and 48 amino acids at its amino and carboxyl terminus, respectively. To better understand the role of the various sequence domains of the MrpS28 protein in vivo, truncated derivatives were expressed under conditions where they were the only potential source of functional MrpS28 protein. The results shown here demonstrate that the amino-terminal domain and the S15-like domain are both essential for respiratory growth. Interestingly an inactive amino-terminal fragment can be complemented in trans by a second inactive fragment comprising the S15-like domain and the carboxyl-terminal 48 amino acids. Consequently, the assembly of these fragments into ribosomal subunits can be examined when they are expressed individually or together. Results from these studies indicate that each of the MrpS28-derived fragments facilitates the incorporation of the other into 37 S ribosomal subunits.