The gene encoding ribosomal protein S14 (rps14) in Oenothera mitochondria is located upstream of the cytochrome b gene (cob). Sequence analysis of independently derived cDNA clones covering the entire rps14 coding region shows two nucleotides edited from the genomic DNA to the mRNA derived

A 2.0-kbp Pst I DNA fragment of the unicellular cyanobacterium Synechococcus sp. strain PCC 6301 genome contains two open reading frames (ORFs). The first ORF of 100 codons potentially encodes a polypeptide having 47 % amino acid identity to Escherichia coli ribosomal protein S14, suggesting

-. The ORF7O3 is composed of 100 codons in which those for lysine (15Z) and arginine (HZ) are abundant, and could be accounted for as a counterpart of E_. coli ribosomal protein S14 since they share 45 % homology in the amino acid sequences. The 0RF701 appears to code for a membrane protein, showing a

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ation, and termination phases of protein synthesis. Because the structures of several DNA and RNA polymerases have been determined at atomic resolution, the mechanisms of DNA and RNA synthesis are both well understood. Determination of the structure of the ribosome, however, has proven a daunting

, Pevzner and Sze introduced algorithms that succeeded. However, their algorithms failed to solve the considerably more difficult (14,4)-, (16,5)-, and (18,6)motif problems. We introduce a novel motif discovery algorithm based on the use of random projections of the input’s substrings. Experiments

lin-4 encodes a small RNA that is complementary to sequences in the 3 � untranslated region (UTR) of lin-14 mRNA and that acts to developmentally repress the accumulation of LIN-14 protein. This repression is essential for the proper timing of numerous events of Caenorhabditis elegans larval

Lysine acetylation is a reversible posttranslational modification of proteins and plays a key role in regulating gene expression. Technological limitations have so far prevented a global analysis of lysine acetylation’s cellular roles. We used high-resolution mass spectrometry to identify 3600

of the fact thatribosomal proteins are assembled in the nucleolus of all cells. Consequently, transgenic mice containing ribosomal protein L10a fused to enhanced green fluorescent protein (EGFP)— for example, the Pcp2 bacTRAP and NeuroD1 bacTRAP lines that express in cerebellar Purkinje and granule neurons

coding microRNAs (miR-143, miR-145). In 5q-syndrome one allele is deleted that accounts for haploinsufficiency of these genes. The mechanism of erythroid failure appears to involve the decreased expression of the ribosomal protein S14 (RPS14) gene and the upregulation of the p53 pathway by ribosomal