Characteristics of physiology of and genomic mutations in aggregation-enhanced mutants of Methanothermobacter sp. CaT2

Figures & data

Table 1. Thicknesses of the cell wall (CW) and sugar layer (SL) in aggregation-enhanced mutants CHA001 and CHA002.

Strain	CW^a	SL^a
			CHA001	11.8 ± 1.5	13.6 ± 0.9
CHA002	6.8 ± 1.1	9.1 ± 1.4
CaT2^b	15.2 ± 1.3	12.7 ± 0.8

^aThe thickness of the layer structure was measured from each TEM image. Standard deviations are indicated after the measurements (n = 7).

^bData from Sumikawa et al. [19].

Figure 1. Images of Methanothermobacter sp. CaT2 and the aggregation-enhanced mutants, CHA001 and CHA002.

Figure 2. Aggregation size of CaT2, CHA001, and CHA002.

Figure 3. Comparison of methane production by CaT2, CHA001, and CHA002.

Figure 4. Effects of proteinase K treatment, DNase treatment and addition of CaCl₂ on the sedimentation indices of CaT2 and CHA001.

Figure 5. Effects of proteinase K treatment, DNase treatment and addition of CaCl₂ on the sedimentation indices of CaT2 and CHA002.

Table 2. Summary of mutations in CHA001 and CHA002.

Position	Gene	Product	Mutation	Amino acid substitution	Amino acid number	CHA001	CHA002
1323438	MTCT_1348	Pyridox-amine 5,-phosph-ate oxidase	Nucleotide substitution T → C	Thr189Ala	313	+	+
354842	MTCT_0393	Cobalt ABC transporter ATP-binding subunit	Nonsence mutation TG → T	Val9Stop	480 to 8	+	−
146492	MTCT_0179	Acetyl-CoA synthetase	Nonsence mutation AG → A	Val73Stop	635 to 72	−	+
436706	MTCT_0445	DUF2085 domain- containing protein	Insertion AAC → ACCAC	Asn13 Frameshit	111 to 50	−	+
1180340	Non-coding	−	Deletion GT → G	−	−	+	+

Sumikawa K, Kosaka T, Mayahara N, et al. An aggregation-defective mutant of Methanothermobacter sp. CaT2 reveals unique protein-dependent aggregation. Microbes Environ. 2019 Sep 25;34:244–251.

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