Complexes with truncated RNAs from the large domain of Archaeoglobus fulgidus signal recognition particle

Shakhawat Hossain Bhuiyan; Olga N. Pakhomova; Andrew P. Hinck; Christian Zwieb

doi:10.1016/S0378-1097(01)00141-0

Complexes with truncated RNAs from the large domain of Archaeoglobus fulgidus signal recognition particle

Shakhawat Hossain Bhuiyan, Olga N. Pakhomova, Andrew P. Hinck, Christian Zwieb

Biochemistry & Structural Biology

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Protein SRP19 is an important component of the signal recognition particle (SRP) as it promotes assembly of protein SRP54 with SRP RNA and recognizes a tetranucleotide loop. Structural features and RNA binding activities of SRP19 of the hyperthermophilic archaeon Archaeoglobus fulgidus were investigated. An updated alignment of SRP19 sequences predicted three conserved regions and two α-helices. With Af-SRP RNA the Af-SRP54 protein assembled into an A. fulgidus SRP which remained intact for many hours. Stable complexes were formed between Af-SRP19 and truncated SRP RNAs, including a 36-residue fragment representing helix 6 of A. fulgidus SRP RNA.

Original language	English (US)
Pages (from-to)	105-110
Number of pages	6
Journal	FEMS Microbiology Letters
Volume	198
Issue number	2
DOIs	https://doi.org/10.1016/S0378-1097(01)00141-0
State	Published - May 1 2001

Keywords

Archaeon
Protein targeting
Protein-RNA interaction
Signal recognition particle

ASJC Scopus subject areas

Microbiology
Molecular Biology
Genetics

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10.1016/S0378-1097(01)00141-0

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title = "Complexes with truncated RNAs from the large domain of Archaeoglobus fulgidus signal recognition particle",

abstract = "Protein SRP19 is an important component of the signal recognition particle (SRP) as it promotes assembly of protein SRP54 with SRP RNA and recognizes a tetranucleotide loop. Structural features and RNA binding activities of SRP19 of the hyperthermophilic archaeon Archaeoglobus fulgidus were investigated. An updated alignment of SRP19 sequences predicted three conserved regions and two α-helices. With Af-SRP RNA the Af-SRP54 protein assembled into an A. fulgidus SRP which remained intact for many hours. Stable complexes were formed between Af-SRP19 and truncated SRP RNAs, including a 36-residue fragment representing helix 6 of A. fulgidus SRP RNA.",

keywords = "Archaeon, Protein targeting, Protein-RNA interaction, Signal recognition particle",

author = "Bhuiyan, {Shakhawat Hossain} and Pakhomova, {Olga N.} and Hinck, {Andrew P.} and Christian Zwieb",

note = "Funding Information: S.H.B. is on research leave from the Department of Microbiology, University of Dhaka, Bangladesh. This work was supported by NIH Grant GM-49034 to C.Z.",

year = "2001",

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doi = "10.1016/S0378-1097(01)00141-0",

language = "English (US)",

volume = "198",

pages = "105--110",

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T1 - Complexes with truncated RNAs from the large domain of Archaeoglobus fulgidus signal recognition particle

AU - Bhuiyan, Shakhawat Hossain

AU - Pakhomova, Olga N.

AU - Hinck, Andrew P.

AU - Zwieb, Christian

N1 - Funding Information: S.H.B. is on research leave from the Department of Microbiology, University of Dhaka, Bangladesh. This work was supported by NIH Grant GM-49034 to C.Z.

PY - 2001/5/1

Y1 - 2001/5/1

N2 - Protein SRP19 is an important component of the signal recognition particle (SRP) as it promotes assembly of protein SRP54 with SRP RNA and recognizes a tetranucleotide loop. Structural features and RNA binding activities of SRP19 of the hyperthermophilic archaeon Archaeoglobus fulgidus were investigated. An updated alignment of SRP19 sequences predicted three conserved regions and two α-helices. With Af-SRP RNA the Af-SRP54 protein assembled into an A. fulgidus SRP which remained intact for many hours. Stable complexes were formed between Af-SRP19 and truncated SRP RNAs, including a 36-residue fragment representing helix 6 of A. fulgidus SRP RNA.

AB - Protein SRP19 is an important component of the signal recognition particle (SRP) as it promotes assembly of protein SRP54 with SRP RNA and recognizes a tetranucleotide loop. Structural features and RNA binding activities of SRP19 of the hyperthermophilic archaeon Archaeoglobus fulgidus were investigated. An updated alignment of SRP19 sequences predicted three conserved regions and two α-helices. With Af-SRP RNA the Af-SRP54 protein assembled into an A. fulgidus SRP which remained intact for many hours. Stable complexes were formed between Af-SRP19 and truncated SRP RNAs, including a 36-residue fragment representing helix 6 of A. fulgidus SRP RNA.

KW - Archaeon

KW - Protein targeting

KW - Protein-RNA interaction

KW - Signal recognition particle

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U2 - 10.1016/S0378-1097(01)00141-0

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AN - SCOPUS:0035338533

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EP - 110

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

SN - 0378-1097

IS - 2

ER -

Complexes with truncated RNAs from the large domain of Archaeoglobus fulgidus signal recognition particle

Abstract

Keywords

ASJC Scopus subject areas

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