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1.
FIGURE 7.

FIGURE 7. From: The Archaeal Lsm Protein Binds to Small RNAs.

Comparison of wild type and lsm deletion strain. Comparison of the growth curves of wild type (dark gray diamonds) and deletion strain (light gray squares) shows that the lsm deletion results in slower growth. The x axis indicates the time of growth in hours.

Susan Fischer, et al. J Biol Chem. 2010 November 5;285(45):34429-34438.
2.
FIGURE 4.

FIGURE 4. From: The Archaeal Lsm Protein Binds to Small RNAs.

Haloferax Lsm binds to RNA. A, the recombinant Lsm protein was incubated with oligo(U)-RNA and subsequently loaded onto nondenaturing PAGE. Lanes c, control reaction without proteins; lanes 200 and 400, incubation with 200 and 400 ng of recombinant Lsm protein, respectively. U15 and U30, incubation with U15-RNA and U30-RNA, respectively. RNA and complex are shown schematically at the right. B, tRNA is also bound by the Lsm protein. Incubation of Lsm with a wheat tRNA fraction shows that Lsm also binds to tRNAs. Lane c, control reaction without protein. Lane L, incubation with 100 ng of Lsm protein. RNA and complex are shown schematically on the right.

Susan Fischer, et al. J Biol Chem. 2010 November 5;285(45):34429-34438.
3.
FIGURE 1.

FIGURE 1. From: The Archaeal Lsm Protein Binds to Small RNAs.

Genomic location of the Lsm protein gene. A, the operon containing the genes for Lsm and L37e is bordered by the gene for a potential hydrolase (HVO_2724) and the gene for an amidophosphoribosyltransferase (HVO_2721). The genomic region is given below in nucleotides. B, the reading frames for the Lsm protein (shown in light gray) and the ribosomal protein L37e (shown in dark gray) overlap by 4 nt (shown in bold type).

Susan Fischer, et al. J Biol Chem. 2010 November 5;285(45):34429-34438.
4.
FIGURE 3.

FIGURE 3. From: The Archaeal Lsm Protein Binds to Small RNAs.

The Lsm protein forms homoheptameric complexes. A, in soft mode native mass spectrometry clearly shows that the Haloferax Lsm protein forms heptameric complexes. Depicted are the charge states of the heptamer. B, under harsh conditions the heptamer completely dissociates into fragments mostly into the monomer. Markers on the x axis indicate the masses of Lsm monomers, dimers, trimers, and tetramers (for z = 1).

Susan Fischer, et al. J Biol Chem. 2010 November 5;285(45):34429-34438.
5.
FIGURE 5.

FIGURE 5. From: The Archaeal Lsm Protein Binds to Small RNAs.

Two Lsm complexes bind to oligo(U)-RNA. A, in soft mode native mass spectrometry shows mostly a ternary complex consisting of two Lsm heptamers bound to one U30-RNA molecule. The charge states of the ternary complex are indicated. In addition, a binary complex could also be detected with a lower signal intensity (shown in gray). B, under harsh conditions the complexes partially dissociate into smaller fragments. As can be clearly seen, the ternary complex does not dissociate stoichiometrically but rather loses a varying number of monomers.

Susan Fischer, et al. J Biol Chem. 2010 November 5;285(45):34429-34438.
6.
FIGURE 2.

FIGURE 2. From: The Archaeal Lsm Protein Binds to Small RNAs.

Differential expression of the lsm gene. A, the transcript levels of the lsm gene in cells grown under different conditions were determined by Northern blot analysis. B, the corresponding agarose gel shows that all of the lanes were loaded with the same amount of RNA. The following conditions were applied: aerobic growth in 2.1 m NaCl at 42 °C (lane 1), at 30 °C (lane 2), and at 48 °C (lane 3); anaerobic, nitrate-respirative growth (lane 4); and 1.5 m NaCl (lane 5).

Susan Fischer, et al. J Biol Chem. 2010 November 5;285(45):34429-34438.
7.
FIGURE 6.

FIGURE 6. From: The Archaeal Lsm Protein Binds to Small RNAs.

The Lsm complex binds to sRNA30. LILBID-MS shows a significant amount of unbound heptamer as well as unbound sRNA30. In addition, a binary complex could be detected preceded by a complex of unexpected size. A second complex of unexpected size was also found, which cannot be explained. However, analysis of the RNA alone also revealed a peak of the expected mass of 42 kDa and a second, unexpected peak. Although further experiments are needed to explain the unexpected peaks, the results clearly show the absence of the ternary complex (two Lsm heptamers: one RNA) with sRNA30, which was the major complex with U30-RNA. In addition, the results confirmed the higher affinity of the Lsm protein to U30-RNA compared with sRNA30, because in the former case the total protein amount was bound in a complex with RNA, whereas in the latter case a considerable fraction of the protein remained unbound.

Susan Fischer, et al. J Biol Chem. 2010 November 5;285(45):34429-34438.

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