9482893

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Subject	Predicate	Object	Context
pubmed-article:9482893	rdf:type	pubmed:Citation	lld:pubmed
pubmed-article:9482893	lifeskim:mentions	umls-concept:C0682475	lld:lifeskim
pubmed-article:9482893	lifeskim:mentions	umls-concept:C0035553	lld:lifeskim
pubmed-article:9482893	lifeskim:mentions	umls-concept:C0033684	lld:lifeskim
pubmed-article:9482893	lifeskim:mentions	umls-concept:C0001128	lld:lifeskim
pubmed-article:9482893	lifeskim:mentions	umls-concept:C0082731	lld:lifeskim
pubmed-article:9482893	lifeskim:mentions	umls-concept:C0936012	lld:lifeskim
pubmed-article:9482893	pubmed:issue	5	lld:pubmed
pubmed-article:9482893	pubmed:dateCreated	1998-4-9	lld:pubmed
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pubmed-article:9482893	pubmed:abstractText	The P-protein complex of eukaryotic ribosomes forms a lateral stalk structure in the active site of the large ribosomal subunit and is thought to assist in the elongation phase of translation by stimulating GTPase activity of elongation factor-2 and removal of deacylated tRNA. The complex in animals, fungi, and protozoans is composed of the acidic phosphoproteins P0 (35 kDa), P1 (11-12 kDa), and P2 (11-12 kDa). Previously we demonstrated by protein purification and microsequencing that ribosomes of maize (Zea mays L.) contain P0, one type of P1, two types of P2, and a distinct P1/P2 type protein designated P3. Here we implemented distance matrices, maximum parsimony, and neighbor-joining analyses to assess the evolutionary relationships between the 12 kDa P-proteins of maize and representative eukaryotic species. The analyses identify P3, found to date only in mono- and dicotyledonous plants, as an evolutionarily distinct P-protein. Plants possess three distinct groups of 12 kDa P-proteins (P1, P2, and P3), whereas animals, fungi, and protozoans possess only two distinct groups (P1 and P2). These findings demonstrate that the P-protein complex has evolved into a highly divergent complex with respect to protein composition despite its critical position within the active site of the ribosome.	lld:pubmed
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pubmed-article:9482893	pubmed:language	eng	lld:pubmed
pubmed-article:9482893	pubmed:journal	http://linkedlifedata.com/r...	lld:pubmed
pubmed-article:9482893	pubmed:citationSubset	IM	lld:pubmed
pubmed-article:9482893	pubmed:chemical	http://linkedlifedata.com/r...	lld:pubmed
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pubmed-article:9482893	pubmed:chemical	http://linkedlifedata.com/r...	lld:pubmed
pubmed-article:9482893	pubmed:status	MEDLINE	lld:pubmed
pubmed-article:9482893	pubmed:month	Mar	lld:pubmed
pubmed-article:9482893	pubmed:issn	0027-8424	lld:pubmed
pubmed-article:9482893	pubmed:author	pubmed-author:SpringerMM	lld:pubmed
pubmed-article:9482893	pubmed:author	pubmed-author:Bailey-Serres...	lld:pubmed
pubmed-article:9482893	pubmed:author	pubmed-author:SzickKK	lld:pubmed
pubmed-article:9482893	pubmed:issnType	Print	lld:pubmed
pubmed-article:9482893	pubmed:day	3	lld:pubmed
pubmed-article:9482893	pubmed:volume	95	lld:pubmed
pubmed-article:9482893	pubmed:owner	NLM	lld:pubmed
pubmed-article:9482893	pubmed:authorsComplete	Y	lld:pubmed
pubmed-article:9482893	pubmed:pagination	2378-83	lld:pubmed
pubmed-article:9482893	pubmed:dateRevised	2009-11-18	lld:pubmed
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