Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques.

Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques. Research Abstract Details 

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Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques. Abstract Text:

M Jiang,S M Sullivan,A K Walker,J R Strahler,P C Andrews,J R Maddock,

Biogenesis of the large ribosomal subunit requires the coordinate assembly of two rRNAs and 33 ribosomal proteins. In vivo, additional ribosome assembly factors, such as helicases, GTPases, pseudouridine synthetases, and methyltransferases, are also critical for ribosome assembly. To identify novel ribosome-associated proteins, we used a proteomic approach (isotope tagging for relative and absolute quantitation) that allows for semiquantitation of proteins from complex protein mixtures. Ribosomal subunits were separated by sucrose density centrifugation, and the relevant fractions were pooled and analyzed. The utility and reproducibility of the technique were validated via a double duplex labeling method. Next, we examined proteins from 30S, 50S, and translating ribosomes isolated at both 16 degrees C and 37 degrees C. We show that the use of isobaric tags to quantify proteins from these particles is an excellent predictor of the particles with which the proteins associate. Moreover, in addition to bona fide ribosomal proteins, additional proteins that comigrated with different ribosomal particles were detected, including both known ribosomal assembly factors and unknown proteins. The ribosome association of several of these proteins, as well as others predicted to be associated with ribosomes, was verified by immunoblotting. Curiously, deletion mutants for the majority of these ribosome-associated proteins had little effect on cell growth or on the polyribosome profiles.

Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques. Publishing Authors By Initials

M Jiang,SM Sullivan,AK Walker,JR Strahler,PC Andrews,JR Maddock,

For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

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Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of bacteriology

VOLUME: 189

Page Numbers: 3434-44

Journal Abbreviation:

ISSN: 0021-9193

DAY: 2

MONTH: 03

YEAR: 2007

Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985120

Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques. Keywords Mesh Terms:

KEYWORDS: Temperature

MESH TERMS: physiology

Chemical & Substance for Abstract: Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques. Information

Substance Name: Ribosomal Proteins

Registry Number: 0

Grant and Affiliation Information for Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques.

AFFILIATION: Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109-1048, USA.

Country: United States

AGENCY: United States PHS

GRANT: P41-18627

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MEDLINETA: J Bacteriol

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