The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Schizosaccharomyces pombe Shu1 (UniProt Q92340; gene shu1+; ORF SPAC1F8.02c) is an iron-regulated, cell-surface heme-binding protein required for assimilation of exogenous hemin/heme and heme analogs when endogenous heme biosynthesis is compromised. Direct biochemical evidence shows Shu1 binds hemin with micromolar affinity (~2.2 µM) and genetic evidence shows shu1 deletion prevents hemin-dependent growth in hem1Δ strains and dramatically reduces uptake of the fluorescent heme analog zinc mesoporphyrin (ZnMP). Shu1 localizes to the plasma membrane under iron starvation and is proposed (in later mechanistic synthesis) to traffic to the vacuole upon hemin exposure, consistent with an endocytic/vacuolar route for heme handling in fission yeast. (mourer2015shu1isa pages 1-2, mourer2015shu1isa pages 11-13, mourer2015shu1isa pages 2-3, ping2024theflavohemoglobinyhb1 pages 1-5)
Heme (iron–protoporphyrin IX) is abundant in animals and can serve as an iron reservoir for microbes, but it is hydrophobic and potentially toxic; therefore, microbes often use dedicated acquisition and trafficking systems. In fungi, heme acquisition is best characterized in pathogenic yeasts such as Candida albicans, which use specialized cell-surface receptors—often CFEM-domain proteins—to bind host heme/hemoglobin and promote internalization. (mourer2015shu1isa pages 11-13)
Based on experimental genetics, microscopy, and biochemistry, Shu1 is best defined as a cell-surface, high-affinity hemin/heme-binding factor enabling utilization of extracellular heme as an iron source in S. pombe. Mourer et al. explicitly describe Shu1 as a cell-surface protein involved in iron acquisition from heme, and demonstrate that Shu1 directly interacts with hemin. (mourer2015shu1isa pages 1-2, mourer2015shu1isa pages 11-13)
Shu1 shows sequence similarity to some Candida heme receptors (e.g., Rbt5/Pga7) and contains a cysteine-rich region important for hemin binding, but its cysteine arrangement is described as non-canonical/partial relative to typical CFEM motifs, suggesting Shu1 represents a divergent or distinct fungal heme-binding strategy compared with canonical CFEM relay systems. (mourer2015shu1isa pages 8-9, mourer2015shu1isa pages 11-13, mourer2019étudedumécanisme pages 93-96)
Primary function: facilitate assimilation of exogenous hemin/heme for iron acquisition.
Substrate evidence:
- hem1Δ strains (blocked in first step of heme biosynthesis) can be used to force dependence on exogenous hemin; under these conditions, growth on hemin and uptake of ZnMP depend on shu1+. (mourer2015shu1isa pages 1-2, mourer2015shu1isa pages 2-3)
- Shu1 does not simply substitute for elemental iron uptake; functional assays indicate specificity for heme/porphyrin assimilation rather than FeCl3 uptake alone. (mourer2019étudedumécanisme pages 84-89)
Purified Shu1(21–200) binds hemin directly:
- Spectral titration shows a Soret shift from ~388–391 nm (hemin alone) to ~407 nm upon Shu1 addition, supporting direct coordination/binding. (mourer2015shu1isa pages 11-13, mourer2019étudedumécanisme pages 89-93)
- Binding analysis yields K_D ≈ 2.2 × 10⁻⁶ M (≈2.2 µM). (mourer2015shu1isa pages 11-13, mourer2019étudedumécanisme pages 89-93)
- Hemin-agarose pulldown experiments show Shu1 is retained on hemin-agarose, supporting specific hemin interaction. (mourer2015shu1isa pages 11-13, mourer2019étudedumécanisme pages 89-93)
Cysteine-dependence:
- Mutation of C72/C87/C92/C101 → Ala strongly reduces hemin-agarose retention and eliminates high-affinity binding behavior, indicating these residues (or a subset) are crucial for heme coordination. (mourer2015shu1isa pages 11-13, mourer2019étudedumécanisme pages 89-93, mourer2019étudedumécanisme pages 93-96)
A key 2024 development is the explicit framing of two distinct exogenous heme uptake pathways in S. pombe: Shu1 (cell-surface/GPI-anchored route) and Str3 (a distinct MFS transporter route). (ping2024theflavohemoglobinyhb1 pages 13-17, ping2024theflavohemoglobinyhb1 pages 10-13)
In that 2024 synthesis, Shu1 is described as:
- a cell-surface GPI-anchored heme receptor that binds hemin or ZnMP, and
- a component of a pathway in which cargo is delivered to the vacuole, followed by redistribution to the cytoplasm via the vacuolar ABC transporter Abc3 (a model consistent with vacuolar involvement in heme/iron handling). (ping2024theflavohemoglobinyhb1 pages 1-5)
This places Shu1 in an iron-acquisition network alongside reductive iron assimilation and siderophore transport but functioning specifically for heme assimilation. (mourer2015shu1isa pages 13-14)
Mourer et al. used HA-tagged Shu1 and found peripheral staining consistent with cell-surface localization under iron starvation; spheroplast experiments support a plasma membrane location rather than exclusive cell wall retention. (mourer2015shu1isa pages 8-9)
The requested visual evidence is present in the 2015 paper figures (immunofluorescence and biochemical fractionation; hemin-binding assays; growth assays). (mourer2015shu1isa media ac014ef9)
A later mechanistic synthesis (2024 preprint) describes Shu1 as being rapidly internalized to the vacuolar membrane after binding hemin/ZnMP, consistent with an endocytic/vacuolar delivery route for porphyrin handling. (ping2024theflavohemoglobinyhb1 pages 1-5)
Shu1 is strongly iron-regulated:
- shu1+ transcription is induced by low iron and repressed by iron repletion in a mechanism involving the GATA-type repressor Fep1. (mourer2015shu1isa pages 1-2, mourer2015shu1isa pages 2-3)
- In 2015, shu1 induction under iron starvation is reported with delayed kinetics: detectable at ~90 min and maximal by ~4 h, slower than some other iron-uptake genes. (mourer2015shu1isa pages 13-14)
In Ping et al. (2024), the shu1+ promoter is used as a positive control for Fep1 ChIP and shows iron-dependent promoter occupancy: ~7.3-fold enrichment under iron-replete vs ~1.2-fold under low iron. (ping2024theflavohemoglobinyhb1 pages 10-13)
Using hem1Δ strains (blocked heme biosynthesis, requiring exogenous heme/ALA), deletion of shu1 compromises hemin utilization:
- A hem1Δ shu1Δ strain shows ~6–8-fold less growth after 68 h than shu1+ controls under hemin-supported conditions (hemin 0.075 µM). (mourer2019étudedumécanisme pages 84-89)
ZnMP uptake is Shu1-dependent:
- Typical assay conditions include iron manipulation by Dip 250 µM or FeCl3 100 µM for 3 h, followed by incubation with ZnMP 2 µM for 90 min; deletion of shu1 dramatically reduces cellular ZnMP signal. (mourer2015shu1isa pages 10-11, mourer2019étudedumécanisme pages 84-89)
Ping et al. (bioRxiv, 2024-03-03) integrates Shu1 into a broader physiological context in which exogenous heme uptake supports heme-dependent processes such as nitrosative stress defense (via Yhb1) when cells rely on external hemin. While their main focus is Str3–Yhb1 interaction, they explicitly treat Shu1 and Str3 as the two distinct heme uptake pathways in fission yeast and provide updated regulatory and trafficking context for Shu1. (ping2024theflavohemoglobinyhb1 pages 1-5, ping2024theflavohemoglobinyhb1 pages 10-13, ping2024theflavohemoglobinyhb1 pages 13-17)
A 2023 review on fungal siderophore metabolism emphasizes that high-affinity iron uptake in many fungi is dominated by reductive iron assimilation and siderophore systems, and notes that some fungi (e.g., Aspergillus fumigatus) appear to lack efficient use of heme as an iron source—highlighting lineage diversity and why a dedicated heme uptake factor like Shu1 may be more relevant in some fungi than others. This review does not discuss Shu1 or CFEM heme receptors directly, so its relevance is contextual rather than Shu1-specific. (happacher2023fungalsiderophoremetabolism pages 1-3)
Shu1 provides a tractable model for:
- Studying fungal heme uptake mechanisms in a genetically manipulable yeast, including cell-surface binding, endocytic routing, and vacuolar redistribution models. (mourer2015shu1isa pages 1-2, ping2024theflavohemoglobinyhb1 pages 1-5)
- Chemical biology/transport assays using fluorescent heme analogs (ZnMP) to quantify uptake dependence on surface factors and iron regulation. (mourer2015shu1isa pages 10-11)
While S. pombe is not a major pathogen, Shu1-like heme acquisition principles connect to heme uptake in pathogenic fungi where cell-surface heme receptors contribute to iron acquisition in host environments. The S. pombe Shu1 system broadens comparative understanding of fungal heme uptake beyond the well-studied Candida CFEM relay. (mourer2015shu1isa pages 11-13, mourer2015shu1isa pages 13-14)
| Category | Key findings | Evidence type | Primary source(s) with publication date and URL |
|---|---|---|---|
| identity/structure | shu1 = SPAC1F8.02c = UniProt Q92340 in Schizosaccharomyces pombe; encodes a 226 aa precursor/cell-surface heme-binding protein with N-terminal signal peptide, predicted GPI-anchor attachment near Ser199, short C-terminal hydrophobic segment/pro-peptide, and a partial CFEM-like cysteine-rich region including C72/C87/C92/C101 important for heme interaction (mourer2015shu1isa pages 1-2, mourer2019étudedumécanisme pages 61-65, mourer2015shu1isa pages 13-14) | Sequence analysis, genetics, biochemistry | Mourer T, Jacques J-F, Brault A, Bisaillon M, Labbé S. 2015-04. Shu1 Is a Cell-surface Protein Involved in Iron Acquisition from Heme in Schizosaccharomyces pombe. J Biol Chem. https://doi.org/10.1074/jbc.m115.642058 ; Mourer T. 2019. Étude du mécanisme d'acquisition de l'hème par le récepteur Shu1 chez Schizosaccharomyces pombe (thesis/monograph record) (mourer2015shu1isa pages 1-2, mourer2019étudedumécanisme pages 61-65, mourer2015shu1isa pages 13-14) |
| substrate specificity | Shu1 is required for utilization of exogenous hemin/heme and uptake of the fluorescent heme analog ZnMP when endogenous heme synthesis is blocked (hem1Δ background). Available evidence supports heme/porphyrin uptake specificity, not general ferric iron uptake; Shu1 does not substitute for the high-affinity elemental iron uptake system and cannot mediate growth on exogenous FeCl3 alone (mourer2019étudedumécanisme pages 84-89, mourer2015shu1isa pages 2-3, mourer2019étudedumécanisme pages 61-65) | Genetics, uptake assay | Mourer et al., 2015-04, https://doi.org/10.1074/jbc.m115.642058 ; Mourer, 2019 (mourer2019étudedumécanisme pages 84-89, mourer2015shu1isa pages 2-3, mourer2019étudedumécanisme pages 61-65) |
| binding affinity | Purified Shu1(21–200) binds hemin directly in vitro. Spectral titration of 10 µM hemin with 0–7 µM Shu1 shifted the Soret peak from ~388–391 nm to ~407 nm and gave an apparent K_D ≈ 2.2 × 10^-6 M (2.2 µM). The C72A/C87A/C92A/C101A mutant greatly reduced hemin-agarose retention and failed to yield a measurable high-affinity interaction (mourer2015shu1isa pages 1-2, mourer2019étudedumécanisme pages 89-93, mourer2015shu1isa pages 11-13) | Biochemistry | Mourer et al., 2015-04, https://doi.org/10.1074/jbc.m115.642058 ; Mourer, 2019 (mourer2015shu1isa pages 1-2, mourer2019étudedumécanisme pages 89-93, mourer2015shu1isa pages 11-13) |
| localization | HA-tagged Shu1 localizes to the cell periphery/plasma membrane under low-iron conditions; localization remains membrane-associated after cell wall digestion (spheroplasts), supporting plasma membrane rather than wall-only localization. Later work indicates Shu1 is hemin-responsive: at low hemin it is at the plasma membrane, while at higher extracellular hemin it is internalized to the vacuole/vacuolar membrane (mourer2015shu1isa pages 8-9, mourer2019étudedumécanisme pages 106-109, mourer2019étudedumécanisme pages 132-135, mourer2015shu1isa media ac014ef9) | Microscopy, membrane fractionation | Mourer et al., 2015-04, https://doi.org/10.1074/jbc.m115.642058 ; Mourer, 2019 (mourer2015shu1isa pages 8-9, mourer2019étudedumécanisme pages 106-109, mourer2019étudedumécanisme pages 132-135, mourer2015shu1isa media ac014ef9) |
| regulation | Iron starvation induces shu1+, whereas iron repletion represses it through the GATA-type repressor Fep1. In the 2015 study, induction was detectable after ~90 min of iron starvation and reached maximal levels by ~4 h. Typical assay conditions included Dip 250 µM or FeCl3 100 µM for 3 h. A 2024 study used the shu1+ promoter as a Fep1 ChIP positive control and reported ~7.3-fold Fep1 enrichment at the promoter under iron-replete conditions versus ~1.2-fold under low iron (mourer2015shu1isa pages 1-2, mourer2015shu1isa pages 13-14, mourer2019étudedumécanisme pages 84-89, mourer2019étudedumécanisme pages 80-84, ping2024theflavohemoglobinyhb1 pages 10-13) | Regulatory, ChIP, expression analysis | Mourer et al., 2015-04, https://doi.org/10.1074/jbc.m115.642058 ; Ping FLY et al. 2024-03. The flavohemoglobin Yhb1 is a new interacting partner of the heme transporter Str3 (preprint). https://doi.org/10.1101/2024.03.03.583214 (mourer2015shu1isa pages 1-2, mourer2015shu1isa pages 13-14, ping2024theflavohemoglobinyhb1 pages 10-13) |
| pathway/model | Best-supported model: Shu1 is a cell-surface GPI-anchored heme receptor/transporter that captures extracellular heme/ZnMP for iron acquisition. Shu1-mediated heme use is independent of Fio1/Fip1 oxidase-permease-mediated elemental iron uptake. Later mechanistic work proposes that Shu1-bound heme is trafficked via endocytosis to the vacuole, followed by export to the cytoplasm through the vacuolar ABC transporter Abc3; this is distinct from the parallel Str3 pathway (mourer2015shu1isa pages 13-14, mourer2019étudedumécanisme pages 106-109, ping2024theflavohemoglobinyhb1 pages 1-5) | Genetics, cell biology, pathway inference | Mourer et al., 2015-04, https://doi.org/10.1074/jbc.m115.642058 ; Ping et al., 2024-03, https://doi.org/10.1101/2024.03.03.583214 ; Mourer, 2019 (mourer2015shu1isa pages 13-14, mourer2019étudedumécanisme pages 106-109, ping2024theflavohemoglobinyhb1 pages 1-5) |
| key assays & phenotypes | In hem1Δ cells (heme biosynthesis blocked), exogenous ALA 200 µM rescues viability and enables heme-uptake assays. In hemin-supported growth conditions (hemin 0.075 µM), hem1Δ shu1Δ cells show severe growth defects; one study reports ~6–8-fold less growth after 68 h than shu1+ controls/complemented strains. ZnMP uptake assays used 2 µM ZnMP after 3 h iron manipulation and 90 min uptake; loss of shu1 dramatically lowered ZnMP fluorescence. Hemin-agarose pull-down and spectral titration support direct binding, while the cysteine-quartet mutant loses function without obvious mislocalization (mourer2019étudedumécanisme pages 84-89, mourer2015shu1isa pages 2-3, mourer2015shu1isa pages 10-11, mourer2015shu1isa media ac014ef9) | Genetics, fluorescence uptake assay, biochemistry, microscopy | Mourer et al., 2015-04, https://doi.org/10.1074/jbc.m115.642058 ; Mourer, 2019 (mourer2019étudedumécanisme pages 84-89, mourer2015shu1isa pages 2-3, mourer2015shu1isa pages 10-11, mourer2015shu1isa media ac014ef9) |
| recent updates 2024 | A 2024 S. pombe preprint places Shu1 in a broader dual heme-uptake network with Str3. It describes Shu1 as the high-affinity/cell-surface GPI-anchored route for hemin/ZnMP uptake and notes mechanistic requirements for Shu1 trafficking/internalization involving Ubi4-dependent ubiquitination, Ubc13, Nbr1, and ESCRT factors (Hse1, Sst6), whereas Str3 is a separate 12-TM transporter route that remains at the plasma membrane and requires higher hemin concentrations than Shu1. This refines pathway context but does not overturn the core 2015 annotation (ping2024theflavohemoglobinyhb1 pages 1-5, ping2024theflavohemoglobinyhb1 pages 10-13, ping2024theflavohemoglobinyhb1 pages 13-17) | Recent mechanistic synthesis, genetics, trafficking model | Ping FLY et al. 2024-03. The flavohemoglobin Yhb1 is a new interacting partner of the heme transporter Str3 (preprint). https://doi.org/10.1101/2024.03.03.583214 (ping2024theflavohemoglobinyhb1 pages 1-5, ping2024theflavohemoglobinyhb1 pages 10-13, ping2024theflavohemoglobinyhb1 pages 13-17) |
Table: This table summarizes experimentally supported functional annotation for fission yeast Shu1/Q92340, including structure, substrate, affinity, localization, regulation, and pathway context. It is designed as a compact evidence map linking each claim to primary sources and available quantitative data.
The 2015 JBC paper includes figures showing: (i) Shu1 plasma membrane localization by immunofluorescence; (ii) hemin-dependent growth assays demonstrating Shu1 requirement; and (iii) hemin-agarose pulldown and spectral titration defining hemin binding (including the KD). (mourer2015shu1isa media ac014ef9)
References
(mourer2015shu1isa pages 1-2): Thierry Mourer, Jean-François Jacques, Ariane Brault, Martin Bisaillon, and Simon Labbé. Shu1 is a cell-surface protein involved in iron acquisition from heme in schizosaccharomyces pombe. Journal of Biological Chemistry, 290:10176-10190, Apr 2015. URL: https://doi.org/10.1074/jbc.m115.642058, doi:10.1074/jbc.m115.642058. This article has 49 citations and is from a domain leading peer-reviewed journal.
(mourer2015shu1isa pages 11-13): Thierry Mourer, Jean-François Jacques, Ariane Brault, Martin Bisaillon, and Simon Labbé. Shu1 is a cell-surface protein involved in iron acquisition from heme in schizosaccharomyces pombe. Journal of Biological Chemistry, 290:10176-10190, Apr 2015. URL: https://doi.org/10.1074/jbc.m115.642058, doi:10.1074/jbc.m115.642058. This article has 49 citations and is from a domain leading peer-reviewed journal.
(mourer2015shu1isa pages 2-3): Thierry Mourer, Jean-François Jacques, Ariane Brault, Martin Bisaillon, and Simon Labbé. Shu1 is a cell-surface protein involved in iron acquisition from heme in schizosaccharomyces pombe. Journal of Biological Chemistry, 290:10176-10190, Apr 2015. URL: https://doi.org/10.1074/jbc.m115.642058, doi:10.1074/jbc.m115.642058. This article has 49 citations and is from a domain leading peer-reviewed journal.
(ping2024theflavohemoglobinyhb1 pages 1-5): Florie Lo Ying Ping, Tobias Vahsen, Ariane Brault, Raphaël Néré, and Simon Labbé. The flavohemoglobin yhb1 is a new interacting partner of the heme transporter str3. BioRxiv, Mar 2024. URL: https://doi.org/10.1101/2024.03.03.583214, doi:10.1101/2024.03.03.583214. This article has 0 citations.
(mourer2015shu1isa pages 8-9): Thierry Mourer, Jean-François Jacques, Ariane Brault, Martin Bisaillon, and Simon Labbé. Shu1 is a cell-surface protein involved in iron acquisition from heme in schizosaccharomyces pombe. Journal of Biological Chemistry, 290:10176-10190, Apr 2015. URL: https://doi.org/10.1074/jbc.m115.642058, doi:10.1074/jbc.m115.642058. This article has 49 citations and is from a domain leading peer-reviewed journal.
(mourer2019étudedumécanisme pages 93-96): T Mourer. Étude du mécanisme d'acquisition de l'hème par le récepteur shu1 chez schizosaccharomyces pombe. Unknown journal, 2019.
(mourer2019étudedumécanisme pages 84-89): T Mourer. Étude du mécanisme d'acquisition de l'hème par le récepteur shu1 chez schizosaccharomyces pombe. Unknown journal, 2019.
(mourer2019étudedumécanisme pages 89-93): T Mourer. Étude du mécanisme d'acquisition de l'hème par le récepteur shu1 chez schizosaccharomyces pombe. Unknown journal, 2019.
(ping2024theflavohemoglobinyhb1 pages 13-17): Florie Lo Ying Ping, Tobias Vahsen, Ariane Brault, Raphaël Néré, and Simon Labbé. The flavohemoglobin yhb1 is a new interacting partner of the heme transporter str3. BioRxiv, Mar 2024. URL: https://doi.org/10.1101/2024.03.03.583214, doi:10.1101/2024.03.03.583214. This article has 0 citations.
(ping2024theflavohemoglobinyhb1 pages 10-13): Florie Lo Ying Ping, Tobias Vahsen, Ariane Brault, Raphaël Néré, and Simon Labbé. The flavohemoglobin yhb1 is a new interacting partner of the heme transporter str3. BioRxiv, Mar 2024. URL: https://doi.org/10.1101/2024.03.03.583214, doi:10.1101/2024.03.03.583214. This article has 0 citations.
(mourer2015shu1isa pages 13-14): Thierry Mourer, Jean-François Jacques, Ariane Brault, Martin Bisaillon, and Simon Labbé. Shu1 is a cell-surface protein involved in iron acquisition from heme in schizosaccharomyces pombe. Journal of Biological Chemistry, 290:10176-10190, Apr 2015. URL: https://doi.org/10.1074/jbc.m115.642058, doi:10.1074/jbc.m115.642058. This article has 49 citations and is from a domain leading peer-reviewed journal.
(mourer2015shu1isa media ac014ef9): Thierry Mourer, Jean-François Jacques, Ariane Brault, Martin Bisaillon, and Simon Labbé. Shu1 is a cell-surface protein involved in iron acquisition from heme in schizosaccharomyces pombe. Journal of Biological Chemistry, 290:10176-10190, Apr 2015. URL: https://doi.org/10.1074/jbc.m115.642058, doi:10.1074/jbc.m115.642058. This article has 49 citations and is from a domain leading peer-reviewed journal.
(mourer2015shu1isa pages 10-11): Thierry Mourer, Jean-François Jacques, Ariane Brault, Martin Bisaillon, and Simon Labbé. Shu1 is a cell-surface protein involved in iron acquisition from heme in schizosaccharomyces pombe. Journal of Biological Chemistry, 290:10176-10190, Apr 2015. URL: https://doi.org/10.1074/jbc.m115.642058, doi:10.1074/jbc.m115.642058. This article has 49 citations and is from a domain leading peer-reviewed journal.
(happacher2023fungalsiderophoremetabolism pages 1-3): Isidor Happacher, Mario Aguiar, Annie Yap, Clemens Decristoforo, and Hubertus Haas. Fungal siderophore metabolism with a focus on aspergillus fumigatus: impact on biotic interactions and potential translational applications. Essays in Biochemistry, 67:829-842, Sep 2023. URL: https://doi.org/10.1042/ebc20220252, doi:10.1042/ebc20220252. This article has 35 citations and is from a peer-reviewed journal.
(mourer2019étudedumécanisme pages 61-65): T Mourer. Étude du mécanisme d'acquisition de l'hème par le récepteur shu1 chez schizosaccharomyces pombe. Unknown journal, 2019.
(mourer2019étudedumécanisme pages 106-109): T Mourer. Étude du mécanisme d'acquisition de l'hème par le récepteur shu1 chez schizosaccharomyces pombe. Unknown journal, 2019.
(mourer2019étudedumécanisme pages 132-135): T Mourer. Étude du mécanisme d'acquisition de l'hème par le récepteur shu1 chez schizosaccharomyces pombe. Unknown journal, 2019.
(mourer2019étudedumécanisme pages 80-84): T Mourer. Étude du mécanisme d'acquisition de l'hème par le récepteur shu1 chez schizosaccharomyces pombe. Unknown journal, 2019.