Archaeal homologs of human rnase p protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 Work on distinct functional domains of the RNA subunit

Takashi Honda, Tadashi Hara, Jinghua Nan, Xjaodong Zhang, Makoto Kimura

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

We examined the functional equivalency between Escherichia coli RNase P protein (C5) and Pyrococcus horikoshii RNase P proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) for RNase P activity. The C5 protein and P. horikoshii RNase P proteins were unable to activate non-congnate RNase P RNAs, P. horikoshii RNase P RNA (PhopRNA) and E. coli RNase P RNA (M1 RNA) respectively. Two chimeric RNAs, in which functional C- and S-domains of M1 RNA and PhopRNA were exchanged, were prepared and characterized with respect to the cleavage of P. horikoshii pre-tRNATyr in the presence of C5 or P. horikoshii proteins. The results suggest that PhoPop5 and PhoRpp30 function equivalently to the C5 protein in the E. coli RNase P, being involved in activation of the PhopRNA C-domain. On the other hand, PhoRpp21 and PhoRpp29 are implicated in stabilization of the PhopRNA S-domain.

Original languageEnglish
Pages (from-to)266-273
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Volume74
Issue number2
DOIs
Publication statusPublished - Mar 1 2010

Fingerprint

Ribonuclease P
Pyrococcus horikoshii
Ribonucleases
RNA
Proteins
Escherichia coli
RNA, Transfer, Tyr

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this

Archaeal homologs of human rnase p protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 Work on distinct functional domains of the RNA subunit. / Honda, Takashi; Hara, Tadashi; Nan, Jinghua; Zhang, Xjaodong; Kimura, Makoto.

In: Bioscience, Biotechnology and Biochemistry, Vol. 74, No. 2, 01.03.2010, p. 266-273.

Research output: Contribution to journalArticle

Honda, Takashi ; Hara, Tadashi ; Nan, Jinghua ; Zhang, Xjaodong ; Kimura, Makoto. / Archaeal homologs of human rnase p protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 Work on distinct functional domains of the RNA subunit. In: Bioscience, Biotechnology and Biochemistry. 2010 ; Vol. 74, No. 2. pp. 266-273.
@article{ef09334bf18243879e4f315891696962,
title = "Archaeal homologs of human rnase p protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 Work on distinct functional domains of the RNA subunit",
abstract = "We examined the functional equivalency between Escherichia coli RNase P protein (C5) and Pyrococcus horikoshii RNase P proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) for RNase P activity. The C5 protein and P. horikoshii RNase P proteins were unable to activate non-congnate RNase P RNAs, P. horikoshii RNase P RNA (PhopRNA) and E. coli RNase P RNA (M1 RNA) respectively. Two chimeric RNAs, in which functional C- and S-domains of M1 RNA and PhopRNA were exchanged, were prepared and characterized with respect to the cleavage of P. horikoshii pre-tRNATyr in the presence of C5 or P. horikoshii proteins. The results suggest that PhoPop5 and PhoRpp30 function equivalently to the C5 protein in the E. coli RNase P, being involved in activation of the PhopRNA C-domain. On the other hand, PhoRpp21 and PhoRpp29 are implicated in stabilization of the PhopRNA S-domain.",
author = "Takashi Honda and Tadashi Hara and Jinghua Nan and Xjaodong Zhang and Makoto Kimura",
year = "2010",
month = "3",
day = "1",
doi = "10.1271/bbb.90550",
language = "English",
volume = "74",
pages = "266--273",
journal = "Bioscience, Biotechnology and Biochemistry",
issn = "0916-8451",
publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",
number = "2",

}

TY - JOUR

T1 - Archaeal homologs of human rnase p protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 Work on distinct functional domains of the RNA subunit

AU - Honda, Takashi

AU - Hara, Tadashi

AU - Nan, Jinghua

AU - Zhang, Xjaodong

AU - Kimura, Makoto

PY - 2010/3/1

Y1 - 2010/3/1

N2 - We examined the functional equivalency between Escherichia coli RNase P protein (C5) and Pyrococcus horikoshii RNase P proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) for RNase P activity. The C5 protein and P. horikoshii RNase P proteins were unable to activate non-congnate RNase P RNAs, P. horikoshii RNase P RNA (PhopRNA) and E. coli RNase P RNA (M1 RNA) respectively. Two chimeric RNAs, in which functional C- and S-domains of M1 RNA and PhopRNA were exchanged, were prepared and characterized with respect to the cleavage of P. horikoshii pre-tRNATyr in the presence of C5 or P. horikoshii proteins. The results suggest that PhoPop5 and PhoRpp30 function equivalently to the C5 protein in the E. coli RNase P, being involved in activation of the PhopRNA C-domain. On the other hand, PhoRpp21 and PhoRpp29 are implicated in stabilization of the PhopRNA S-domain.

AB - We examined the functional equivalency between Escherichia coli RNase P protein (C5) and Pyrococcus horikoshii RNase P proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) for RNase P activity. The C5 protein and P. horikoshii RNase P proteins were unable to activate non-congnate RNase P RNAs, P. horikoshii RNase P RNA (PhopRNA) and E. coli RNase P RNA (M1 RNA) respectively. Two chimeric RNAs, in which functional C- and S-domains of M1 RNA and PhopRNA were exchanged, were prepared and characterized with respect to the cleavage of P. horikoshii pre-tRNATyr in the presence of C5 or P. horikoshii proteins. The results suggest that PhoPop5 and PhoRpp30 function equivalently to the C5 protein in the E. coli RNase P, being involved in activation of the PhopRNA C-domain. On the other hand, PhoRpp21 and PhoRpp29 are implicated in stabilization of the PhopRNA S-domain.

UR - http://www.scopus.com/inward/record.url?scp=77249144829&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77249144829&partnerID=8YFLogxK

U2 - 10.1271/bbb.90550

DO - 10.1271/bbb.90550

M3 - Article

VL - 74

SP - 266

EP - 273

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 2

ER -