Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by O'Brien, T. W.
Right arrow Articles by Graack, H.-R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by O'Brien, T. W.
Right arrow Articles by Graack, H.-R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 274, Issue 51, 36043-36051, December 17, 1999

Mammalian Mitochondrial Ribosomal Proteins (2)
AMINO ACID SEQUENCING, CHARACTERIZATION, AND IDENTIFICATION OF CORRESPONDING GENE SEQUENCES*

Thomas W. O'BrienDagger , Scott E. FieslerDagger , Nancy D. DenslowDagger , Bernd Thiede§, Brigitte Wittmann-Liebold§, Edward B. Mougey, James E. Sylvester, and Hanns-Rüdiger Graack||**

From the Dagger  Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, Florida 32610-0245, § Max-Delbrück-Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13125 Berlin, Germany,  Nemours Children's Clinic, Research, Jacksonville, Florida 32207, and the || Institute for Biology-Genetics, AG Kress, Free University of Berlin, Arnimallee 7, D-14195 Berlin, Germany

Four different classes of mammalian mitochondrial ribosomal proteins were identified and characterized. Mature proteins were purified from bovine liver and subjected to N-terminal or matrix-assisted laser-desorption mass spectroscopic amino acid sequencing after tryptic in-gel digestion and high pressure liquid chromatography separation of the resulting peptides. Peptide sequences obtained were used to virtually screen expressed sequence tag data bases from human, mouse, and rat. Consensus cDNAs were assembled in silico from various expressed sequence tag sequences identified. Deduced mammalian protein sequences were characterized and compared with ribosomal protein sequences of Escherichia coli and yeast mitochondria. Significant sequence similarities to ribosomal proteins of other sources were detected for three out of four different mammalian protein classes determined. However, the sequence conservation between mitochondrial ribosomal proteins of mammalian and yeast origin is much less than the sequence conservation between cytoplasmic ribosomal proteins of the same species. In particular, this is shown for the mammalian counterparts of the E. coli EcoL2 ribosomal protein (MRP-L14), that do not conserve the specific and functional highly important His229 residue of E. coli and the corresponding yeast mitochondrial Rml2p.

* This work was supported by United States Public Health Service Grant GM15438 (to T. W. O.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) S78756 (MRP-L5bov), S78757 (MRP-L7bov), S78758 (MRP-L14bov), and S78759 (MRP-L26bov), respectively.

** To whom correspondence should be addressed: Inst. for Biology-Genetics, AG Kress, Free University of Berlin, Arnimallee 7, D-14195 Berlin, Germany. Tel.: 49-30-838-2629; Fax: 49-30-838-3649; E-mail: graack@zedat.fu-berlin.de.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 GENES CELLSHome page
Y. Nozaki, N. Matsunaga, T. Ishizawa, T. Ueda, and N. Takeuchi
HMRF1L is a human mitochondrial translation release factor involved in the decoding of the termination codons UAA and UAG.
Genes Cells, May 1, 2008; 13(5): 429 - 438.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P. Smits, J. A. M. Smeitink, L. P. van den Heuvel, M. A. Huynen, and T. J. G. Ettema
Reconstructing the evolution of the mitochondrial ribosomal proteome
Nucleic Acids Res., July 9, 2007; 35(14): 4686 - 4703.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
E. Teyssier, G. Hirokawa, A. Tretiakova, B. Jameson, A. Kaji, and H. Kaji
Temperature-sensitive mutation in yeast mitochondrial ribosome recycling factor (RRF)
Nucleic Acids Res., July 15, 2003; 31(14): 4218 - 4226.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. C. Koc, W. Burkhart, K. Blackburn, M. B. Moyer, D. M. Schlatzer, A. Moseley, and L. L. Spremulli
The Large Subunit of the Mammalian Mitochondrial Ribosome. ANALYSIS OF THE COMPLEMENT OF RIBOSOMAL PROTEINS PRESENT
J. Biol. Chem., November 16, 2001; 276(47): 43958 - 43969.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. C. Koc, W. Burkhart, K. Blackburn, A. Moseley, H. Koc, and L. L. Spremulli
A Proteomics Approach to the Identification of Mammalian Mitochondrial Small Subunit Ribosomal Proteins
J. Biol. Chem., October 13, 2000; 275(42): 32585 - 32591.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Yamaguchi and A. R. Subramanian
The Plastid Ribosomal Proteins. IDENTIFICATION OF ALL THE PROTEINS IN THE 50 S SUBUNIT OF AN ORGANELLE RIBOSOME (CHLOROPLAST)
J. Biol. Chem., September 8, 2000; 275(37): 28466 - 28482.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. B. Patel, C. C. Cunningham, and R. R. Hantgan
Physiochemical Properties of Rat Liver Mitochondrial Ribosomes
J. Biol. Chem., February 23, 2001; 276(9): 6739 - 6746.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Valgardsdottir, G. Brede, L. G. Eide, E. Frengen, and H. Prydz
Cloning and Characterization of MDDX28, a Putative DEAD-box Helicase with Mitochondrial and Nuclear Localization
J. Biol. Chem., August 17, 2001; 276(34): 32056 - 32063.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Suzuki, M. Terasaki, C. Takemoto-Hori, T. Hanada, T. Ueda, A. Wada, and K. Watanabe
Structural Compensation for the Deficit of rRNA with Proteins in the Mammalian Mitochondrial Ribosome. SYSTEMATIC ANALYSIS OF PROTEIN COMPONENTS OF THE LARGE RIBOSOMAL SUBUNIT FROM MAMMALIAN MITOCHONDRIA
J. Biol. Chem., June 8, 2001; 276(24): 21724 - 21736.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Suzuki, M. Terasaki, C. Takemoto-Hori, T. Hanada, T. Ueda, A. Wada, and K. Watanabe
Proteomic Analysis of the Mammalian Mitochondrial Ribosome. IDENTIFICATION OF PROTEIN COMPONENTS IN THE 28 S SMALL SUBUNIT
J. Biol. Chem., August 24, 2001; 276(35): 33181 - 33195.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. W. O'Brien, J. Liu, J. E. Sylvester, E. B. Mougey, N. Fischel-Ghodsian, B. Thiede, B. Wittmann-Liebold, and H.-R. Graack
Mammalian Mitochondrial Ribosomal Proteins (4). AMINO ACID SEQUENCING, CHARACTERIZATION, AND IDENTIFICATION OF CORRESPONDING GENE SEQUENCES
J. Biol. Chem., June 9, 2000; 275(24): 18153 - 18159.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement