PMID- 10600119
OWN - NLM
STAT- MEDLINE
DCOM- 20000119
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 38
IP  - 50
DP  - 1999 Dec 14
TI  - Identification of mammalian mitochondrial ribosomal proteins (MRPs) by N-terminal
      sequencing of purified bovine MRPs and comparison to data bank sequences: the
      large subribosomal particle.
PG  - 16569-77
AB  - Bovine mitochondrial ribosomes are presented as a model system for mammalian
      mitochondrial ribosomes. An alternative system for identifying individual bovine 
      mitochondrial ribosomal proteins (MRPs) by RP-HPLC is described. To identify and 
      to characterize individual MRPs proteins were purified from bovine liver,
      separated by RP-HPLC, and identified by 2D PAGE techniques and immunoblotting.
      Molecular masses of individual MRPs were determined. Selected proteins were
      subjected to N-terminal amino acid sequencing. The peptide sequences obtained
      were used to screen different databases to identify several corresponding MRP
      sequences from human, mouse, rat, and yeast. Signal sequences for mitochondrial
      import were postulated by comparison of the bovine mature N-termini determined by
      amino acid sequencing with the deduced mammalian MRP sequences. Significant
      sequence similarities of these new MRPs to known r-proteins from other sources,
      e.g., E. coli, were detected only for two of the four MRP families presented.
      This finding suggests that mammalian mitochondrial ribosomes contain several
      novel proteins. Amino acid sequence information for all of the bovine MRPs will
      prove invaluable for assigning functions to their genes, which would otherwise
      remain unknown.
FAU - Graack, H R
AU  - Graack HR
AD  - Department of Biochemistry and Molecular Biology, College of Medicine, University
      of Florida, Gainesville 32610-0245, USA.
FAU - Bryant, M L
AU  - Bryant ML
FAU - O'Brien, T W
AU  - O'Brien TW
LA  - eng
SI  - SWISSPROT/S78750
SI  - SWISSPROT/S78751
SI  - SWISSPROT/S78752
SI  - SWISSPROT/S78753
GR  - GM15438/GM/NIGMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Peptide Fragments)
RN  - 0 (Ribosomal Proteins)
RN  - 0 (ribosomal protein L15)
RN  - 0 (ribosomal protein L2)
RN  - 0 (ribosomal protein L3)
RN  - 0 (ribosomal protein L31)
RN  - 0 (ribosomal protein L34)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cattle
MH  - Humans
MH  - Mice
MH  - Mitochondria/*chemistry
MH  - Molecular Sequence Data
MH  - Peptide Fragments/chemistry/isolation & purification
MH  - Rats
MH  - Ribosomal Proteins/chemistry/*isolation & purification
MH  - Sequence Alignment
MH  - Sequence Analysis, Protein
MH  - Sequence Homology, Amino Acid
MH  - Submitochondrial Particles/chemistry
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - bi991543s [pii]
AID - 10.1021/bi991543s [doi]
PST - ppublish
SO  - Biochemistry. 1999 Dec 14;38(50):16569-77. doi: 10.1021/bi991543s.