LSm proteins form heptameric rings that bind to RNA via repeating motifs

Khusial, P. Raaj; Plaag, Robert; Zieve, Gary W.

doi:10.1016/j.tibs.2005.07.006

Cited by 107 publications

(118 citation statements)

References 54 publications

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“…A first gene duplication event likely created eight distinct Lsm proteins, from which later evolved the Sm protein group. The diversity of biological activities of Lsm proteins compared to their more specialized Sm counterparts supports this two-step evolution model (Beggs, 2005;Khusial et al, 2005). The presence of up to three Lsm proteins in archaea, as well as an Hfq-like protein in archaeal M. jannaschii, further supports a common ancestor of eukaryotic and archaeal Lsm proteins (Fischer et al, 2011).…”

Section: Phylogeny Of Lsm Protein Sequencessupporting

confidence: 52%

“…The following Lsm-Sm protein paralogs are identifiable: Lsm1-SmB, Lsm2-SmD1, Lsm3-SmD2, Lsm4-SmD3, Lsm5-SmE, Lsm6-SmF, Lsm7-SmG, Lsm8-SmB (Fromont-Racine et al, 2000). These specific sequence relationships suggest the eukaryotic Lsm proteins to have evolved from a common archaeal ancestor in two waves (Khusial et al, 2005;Veretnik et al, 2009). A first gene duplication event likely created eight distinct Lsm proteins, from which later evolved the Sm protein group.…”

Section: Phylogeny Of Lsm Protein Sequencesmentioning

confidence: 99%

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The Lsm Proteins: Ring Architectures for RNA Capture

Moll¹,

Sobti²,

Mabbutt³

2011

RNA Processing

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Section: Phylogeny Of Lsm Protein Sequencessupporting

confidence: 52%

Section: Phylogeny Of Lsm Protein Sequencesmentioning

confidence: 99%

The Lsm Proteins: Ring Architectures for RNA Capture

Moll¹,

Sobti²,

Mabbutt³

2011

RNA Processing

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“…2A). Eukaryotic Lsm domain-containing proteins (Lsm proteins) form heteroheptameric rings that bind to single-stranded RNA and are involved in various steps of RNA metabolism (41,42). The Lsm1-7 ring occurs in the cytoplasm and functions as a decapping activator during mRNA degradation.…”

Section: Identification Of the Components Of Frgy2-associatedmentioning

confidence: 99%

RAP55, a Cytoplasmic mRNP Component, Represses Translation in Xenopus Oocytes

Tanaka

Ogawa

Takagi

et al. 2006

Journal of Biological Chemistry

106

128

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mRNAs in eukaryotic cells are presumed to always associate with a set of proteins to form mRNPs. In Xenopus oocytes, a large pool of maternal mRNAs is masked from the translational apparatus as storage mRNPs. Here we identified Xenopus RAP55 (xRAP55) as a component of RNPs that associate with FRGY2, the principal component of maternal mRNPs. RAP55 is a member of the Scd6 or Lsm14 family. RAP55 localized to cytoplasmic foci in Xenopus oocytes and the processing bodies (P-bodies) in cultured human cells: in the latter cells, RAP55 is an essential constituent of the P-bodies. We isolated xRAP55-containing complexes from Xenopus oocytes and identified xRAP55-associated proteins, including a DEAD-box protein, Xp54, and a protein arginine methyltransferase, PRMT1. Recombinant xRAP55 repressed translation, together with Xp54, in an in vitro translation system. In addition, xRAP55 repressed translation in oocytes when tethered with a reporter mRNA. Domain analyses revealed that the N-terminal region of RAP55, including the Lsm domain, is important for the localization to P-bodies and translational repression. Taken together, our results suggest that xRAP55 is involved in translational repression of mRNA as a component of storage mRNPs.

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“…Archaeal genomes usually encode either a single or a few small Sm-related proteins. These form homo-hexameric or homo-heptameric rings and share oligomerization behavior and RNA-binding properties with their eukaryotic counterparts (for reviews, see Pannone and Wolin 2000;Beggs 2005;Khusial et al 2005;Wilusz and Wilusz 2005). The function of the archaeal proteins is currently not clear.…”

Section: Introductionmentioning

confidence: 99%

An Hfq-like protein in archaea: Crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii

Nielsen¹,

Bøggild²,

Andersen³

et al. 2007

RNA

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The Sm and Sm-like proteins are conserved in all three domains of life and have emerged as important players in many different RNA-processing reactions. Their proposed role is to mediate RNA-RNA and/or RNA-protein interactions. In marked contrast to eukaryotes, bacteria appear to contain only one distinct Sm-like protein belonging to the Hfq family of proteins. Similarly, there are generally only one or two subtypes of Sm-related proteins in archaea, but at least one archaeon, Methanococcus jannaschii, encodes a protein that is related to Hfq. This archaeon does not contain any gene encoding a conventional archaeal Sm-type protein, suggesting that Hfq proteins and archaeal Sm-homologs can complement each other functionally. Here, we report the functional characterization of M. jannaschii Hfq and its crystal structure at 2.5 Å resolution. The protein forms a hexameric ring. The monomer fold, as well as the overall structure of the complex is similar to that found for the bacterial Hfq proteins. However, clear differences are seen in the charge distribution on the distal face of the ring, which is unusually negative in M. jannaschii Hfq. Moreover, owing to a very short N-terminal a-helix, the overall diameter of the archaeal Hfq hexamer is significantly smaller than its bacterial counterparts. Functional analysis reveals that Escherichia coli and M. jannaschii Hfqs display very similar biochemical and biological properties. It thus appears that the archaeal and bacterial Hfq proteins are largely functionally interchangeable.

show abstract

LSm proteins form heptameric rings that bind to RNA via repeating motifs

Cited by 107 publications

References 54 publications

The Lsm Proteins: Ring Architectures for RNA Capture

The Lsm Proteins: Ring Architectures for RNA Capture

RAP55, a Cytoplasmic mRNP Component, Represses Translation in Xenopus Oocytes

An Hfq-like protein in archaea: Crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii

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